​Microscopy​​:​

​Light​​Microscope​ ​Electron​​microscope​​(EM)​ ​Laser​​Scanning​​confocal​

​microscope​

​ sed​​to​​view​​large​​structures​​(e.g​​a​
U ​ ses​​electrons​​to​​form​​images,​​used​​to​​observe​​small​​structures​
U ​ igh​​resolution​
H
​whole​​cell)​ ​(e.g​​cell​​membranes,​​ribosomes)​ ​3D​
​Laser​​light​​used​​to​​create​
​1.​ L ​ ight​​passes​​through​​a​ ​ esolution​​:​​0.2​​nm​
R ​image​
​specimen​​on​​a​​slide.​ ​Magnification​​:​​x​​1,000,000​
​2.​ ​Lenses​​focus​​the​​light​​to​ ​Black​​and​​white​​images​
​form​​a​​magnified​​image​ ​Can​​use​​live​​specimens​​(under​​vacuum​​pressure​​-​​will​​kill​​it)​
​3.​ ​Higher​​magnification​​-​
​switch​​to​​a​​higher​ ​Transmission​​electron​ ​Scanning​​electron​
​objective​​lens​ ​microscopes​​(TEM)​ ​microscopes​​(SEM)​

​ esolution​​:​​Poor​​-​​200​​nm​​(due​​to​
R ​ se​​electromagnets​​to​​transmit​​a​
U ​ ass​​beam​​of​​electrons​
P
​wavelength​​of​​light)​ ​beam​​of​​electrons​​through​​a​ ​across​​the​​surface​​of​
​Magnification​​:​​x​​1500​ ​specimen,​​denser​​parts​​absorb​ ​specimen,​​detects​​the​​rate​​at​
​Coloured​​images​ ​more​​electrons​​(darker)​ ​which​​electrons​​bounce​​back​
​Can​​use​​living​​specimens​
​ igh​​resolution​
H ​ ower​​resolution​​than​​TEM​
L
​Shows​​internal​​structures​ ​Shows​​surfaces​
​2D​ ​3D​

​Resolution​​:​
​ esolution​​-​​The​​ability​​to​​distinguish​​between​​Ptwo​​objects​​in​​which​​they​​can​​still​​be​​viewed​
R
​as​​separate​
​Optical​​/​​Light​​-​​Limited​​by​​wavelength​​of​​light​​(diffracts​​when​​hits​​small​​objects)​​(if​​objects​​are​
​close​​light​​waves​​overlap​​and​​it's​​hard​​to​​tell​​them​​apart​
​Electron​​-​​Determined​​by​​wavelength​​of​​the​​beam​​of​​electrons​​(objects​​can​​be​​much​​closer​
​together​​before​​the​​diffracted​​electron​​beams​​overlap)​

​Magnification​​:​
​Magnification​​-​​The​​number​​of​​times​​large​​an​​image​​is​​compared​​to​​the​​actual​​object​

​ m​​=​​1000​​mm​
1
​1mm​​=​​1000​​µm​
​1​​µm​​=​​1000​​nm​

​Slide​​preparation​​:​
​ ry​​mount​​-​​Thin​​slices​​or​​whole​​specimen​​are​​viewed​​(just​​place​​a​​coverslip​​on​​top)​
D
​Wet​​mount​​-​​Water​​is​​added​​to​​specimen​​before​​adding​​coverslip​​with​​mounted​​needle​​to​​prevent​​air​​bubbles​​forming.​
​Squash​​slide​​-​​Wet​​mounts,​​then​​push​​down​​a​​coverslip​​for​​a​​thin​​layer​​for​​light​​to​​pass​​through​​(what​​you​​do​​to​​view​​a​​root​​tip)​
​Smear​​slides​​-​​Place​​a​​drop​​of​​the​​sample​​at​​one​​end​​and​​use​​edge​​of​​another​​slide​​to​​smear​​sample​​across​​first​​slide,​​add​​cover​​slip​

​Eyepiece​​graticule​​&​​calibration​​:​
-​ ​ ​ raticule​​:​​Eyepiece​​ruler​​(no​​fixed​​units)​
G
​-​ ​Calibrate​​with​​stage​​micrometer​​(Each​​division​​10µm)​
​-​ ​Once​​calibrated,​​graticule​​gives​​accurate​​measurements​​of​​specimen​

​Calibration​​:​
​ .​ L
1 ​ ine​​up​​stage​​micrometer​​and​​eyepiece​​graticule​​whilst​​looking​​through​​eyepiece​
​2.​ ​Count​​how​​many​​divisions​​on​​the​​eyepiece​​graticule​​fit​​into​​one​​division​​on​​the​​micrometer​​scale​
​3.​ ​Each​​division​​on​​the​​micrometer​​is​​10µm,​​so​​this​​is​​used​​to​​calculate​​what​​one​​division​​on​​the​
​eyepiece​​graticule​​is​​at​​that​​magnification.​

​Staining​​in​​Microscopy​​:​
​ ight​​-​​Stain​​absorbs​​light,​​making​​structures​​more​​visible.​​Some​​structures​​have​​more​​of​​an​​affinity​​for​​different​​stains,​​so​​different​​stains​​are​
L
​used​​for​​different​​structures.​
​Electron​​-​​Electrons​​have​​no​​colour​​and​​use​​heavy-metal​​stains​​(E.g,​​osmium​​tetroxide).​​Images​​are​​black/grey,​​colour​​is​​added​​after​
​Cell​​structure​​:​
-​ ​ ​ etailed​​structure​​of​​cells​​is​​called​​the​​ultrastructure​
D
​-​ ​Obtained​​using​​a​​microscope​

​Eukaryotic​​cells​​:​

​Cell​​surface​​membrane​​:​
​-​ ​Controls​​exchange​​of​​materials​​between​​internal​​cell​​environment​​and​​external​
​-​ ​Partially​​permeable​
​-​ ​Forms​​a​​phospholipid​​bilayer​​of​​phospholipids​​spanning​​a​​diameter​​of​​around​​10​​nm​

​Cell​​wall​​(Only​​in​​plants)​​:​
​-​ ​Provides​​structure​​and​​support​
​-​ ​Made​​of​​cellulose​​in​​plants​
​-​ ​Made​​of​​peptidoglycan​​in​​most​​bacteria​
​-​ ​Plasmodesmata​​:​​narrow​​strands​​of​​cytoplasm​​(with​​membrane)​​that​​connect​
​neighbouring​​plant​​cells​​through​​cell​​wall​

​Nucleus​​:​
​-​ ​In​​all​​eukaryotic​​cells​​(except​​RBCs)​
​-​ ​Surrounded​​by​​a​​double​​membrane​​called​​the​​envelope,​​contains​​pores​
​-​ ​Enable​​molecules​​to​​enter​​and​​leave​​the​​nucleus​
​-​ ​Allows​​mRNA​​and​​ribosomes​​to​​exit​
​-​ ​Allows​​enzymes​​(e.g​​DNA​​polymerase)​​and​​signals​​to​​enter​
​-​ ​Contains​​chromatin,​​made​​of​​linear​​DNA​​tightly​​wound​​around​​histone​​proteins​
​-​ ​Nucleolus,​​site​​of​​ribosome​​production,​​one​​or​​more​​visible​​per​​nucleus​

​Mitochondria​​:​
​-​ ​Oval​​shaped,​​bound​​by​​a​​double​​membrane​​called​​the​​envelope​
​-​ ​Inner​​membrane​​folded​​to​​form​​projections​​called​​cristae​
​-​ ​Matrix​​on​​inside​​of​​cristae​​containing​​enzymes​​for​​respiration​​(to​​produce​​ATP)​​and​
​mitochondrial​​DNA​​and​​ribosomes​​for​​replication​​and​​protein​​synthesis​

​Chloroplasts​​:​
​-​ ​Larger​​than​​mitochondria,​​with​​a​​double​​membrane​
​-​ ​Contains​​thylakoids​​(folded​​membrane​​embedded​​with​​pigment)​​stacked​​into​​grana.​
​-​ ​Grana​​are​​concentrated​​by​​lamellae​​(flat​​thylakoid​​membranes​
​-​ ​Light-independent​​stage​​(Calvin​​Cycle)​​:​​in​​the​​stroma​
​-​ ​Contain​​circular​​DNA​​and​​ribosomes​​for​​replication​​and​​protein​​synthesis.​
​Ribosomes​​:​
​-​ ​Found​​in​​all​​cells​​either​​free​​in​​cytoplasm​​or​​on​​the​​rough​​ER​​(in​​eukaryotes)​
​-​ ​Made​​of​​rNA​​and​​proteins​
​-​ ​Types​
​-​ ​80s​​in​​eukaryotic​​cells​
​-​ ​70s​​in​​prokaryotes,​​mitochondria​​and​​chloroplasts​
​-​ ​Site​​of​​translation​​(protein​​synthesis)​

​ ndoplasmic​​reticulum​​(Plant​​&​​animal)​​:​
E
​Rough​​ER​​:​
​-​ ​Has​​a​​golden​​membrane​​called​​cisternae​
​-​ ​Series​​of​​flattened​​sacs​​enclosed​​by​​a​​membrane​​with​​ribosomes​​on​​the​​surface​
​-​ ​Folds​​and​​processes​​proteins​​made​​on​​ribosomes​​for​​transport​​to​​golgi​​apparatus​

​Smooth​​ER​​:​
​-​ ​Produces​​and​​processes​​lipids​
​-​ ​Syntheses​​and​​stores​​lipids,​​carbohydrates​​and​​steroids​

​Golgi​​apparatus​​:​
​-​ ​Folded​​membranes​​making​​cisterne​
​-​ ​Fluid​​filled,​​flattened​​and​​curved​​sacs​​with​​vesicles​​surrounding​​edges​
​-​ ​Processes​​and​​packages​​proteins​​and​​lipids​​(into​​vesicles)​
​-​ ​Produces​​lysosomes​

​Large​​permanent​​vacuole​​:​
​-​ ​A​​sac​​in​​plant​​cells​​(surrounded​​by​​tonoplast)​
​-​ ​Selectively​​permeable​​membrane​
​-​ ​Vacuoles​​in​​animal​​cells​​are​​not​​permanent​​and​​small​

​Vesicles​​:​
​-​ ​Found​​in​​plant​​and​​animal​​cells​
​-​ ​A​​membrane-bound​​sac​​for​​transport​​and​​storage​

​Lysosomes​​:​
​-​ ​A​​vesicle​​containing​​digestive​​enzymes​
​-​ ​Break​​down​​waste​​(E.g,​​worn​​out​​organelles)​
​-​ ​Important​​in​​immune​​response​​and​​apoptosis​​(programmed​​cell​​death)​
​Centrioles​​(Not​​found​​in​​flowering​​plants​​and​​fungi)​​:​
​-​ ​Hollow​​cylinders​​containing​​a​​ring​​of​​microtubules​
​-​ ​Two​​centrioles​​arranged​​at​​right​​angles​​to​​each​​other​​to​​form​​a​​centrosome​
​-​ ​Involved​​in​​cell​​division​
​-​ ​Involved​​in​​production​​of​​spindle​​fibres​​and​​organisation​​of​​chromosomes​​in​
​cell​​division​

​Microtubules​​:​
​-​ ​Found​​in​​all​​eukaryotic​​cells,​​-​​25​​nm​​diameter​
​-​ ​Made​​from​​α-​​and​​𝛽-tubulin​​dimers​​→​​form​​protofilaments​
​-​ ​13​​protofilaments​​form​​a​​cylindrical​​microtubule​
​-​ ​Part​​of​​cytoskeleton​​:​​provides​​cell​​support​​and​​enables​​movement​

​Microvilli​​:​
​-​ ​Found​​in​​specialized​​animal​​cells​
​-​ ​Cell​​membrane​​projections​
​-​ ​Used​​to​​increase​​surface​​area​​of​​cell​​surface​​membrane​​in​​order​​to​​increase​​rate​​of​
​substance​​exchange​

​Cilia​​:​
​-​ H ​ air​​like​​projections​​made​​from​​microtubules​
​-​ ​Allows​​movement​​of​​substances​​over​​cell​​surface​

​(Along​​trachea)​

​Flagella​​:​
​-​ ​Found​​in​​specialised​​cells​
​-​ ​Made​​of​​longer​​microtubules​
​-​ ​Contract​​to​​provide​​cell​​movements​​(E.g,​​in​​sperm​​cells)​

​Cytoskeleton​​:​
​-​ ​Plays​​important​​role​​in​​providing​​mechanical​​strength​
​-​ ​Aids​​transport​​within​​cells​
​-​ ​Enables​​cell​​movement​
​Productions​​and​​transport​​of​​proteins​​:​
​Nucleus​​:​
​-​ ​DNA​​is​​stored,​​Transcription​​:​​DNA​​→​​mRNA,​​Makes​​ribosomes​
​Ribosomes​​:​
​-​ ​(Where​​proteins​​are​​produced)​​mRNA​​leaves​​the​​nucleus​​and​​attaches​​to​​ribosome,​
​Translation​​:​​mRNA​​→​​polypeptide​​chain​​(amino​​acids)​
​Rough​​endoplasmic​​reticulum​​(RER)​​:​
​-​ ​Folds​​and​​processes​​polypeptides​​into​​proteins​
​Golgi​​apparatus​​:​
​-​ ​Proteins​​are​​modified​​and​​packaged​​for​​secretion​
​Vesicles​​:​
​-​ ​Transport​​proteins​​from​​RER​​→​​Golgi​​apparatus​​→​​Cell​​surface​​membrane,​​Exocytosis​​:​​vesicles​​fuse​​with​​membrane​​and​​release​
​proteins​​(E.g​​hormones)​

​Prokaryotic​​cells​
-​ ​ ​ o​​membrane-bound​​organelles​​in​​cytoplasm​
N
​-​ ​No​​nucleus​
​-​ ​Cell​​division​​-​​occurs​​by​​binary​​fission​
​Cell​​wall​​:​
​-​ ​Rigid​​outer​​covering​
​-​ ​Made​​of​​peptidoglycan​

​Capsule​​(Slime​​layer)​​:​
​-​ ​Protective​​slimy​​layer​
​-​ ​Helps​​the​​cell​​to​​retain​​moisture​​and​​to​​adhere​​to​​surfaces​

​Plasmid​​:​
​-​ ​Small​​circular​​DNA​​loops​​separate​​from​​main​​DNA​
​-​ ​Often​​carry​​genes​​like​​antibiotic​​resistance​
​-​ ​Can​​be​​shared​​between​​prokaryotes​

​Flagellum​​:​
​-​ ​Tail-like​​structure​​for​​movement​
​-​ ​Rotates,​​like​​a​​propeller,​​to​​move​​the​​cell​
​-​ ​Some​​prokaryotes​​have​​multiple​​flagella​

​Pilli​​:​
​-​ ​ air-like​​structures​
H
​-​ ​Attach​​to​​other​​bacterial​​cells​

​Ribosomes​​:​
​-​ ​70s​​ribosomes​​(smaller)​
​-​ ​Sight​​of​​protein​​production​
​Biological​​Molecules​​:​

​Water​​:​
​Major​​component​​of​​cells​​(70​​-​​95​​%​​of​​cell​​mass)​

​Structure​​:​
​-​ ​Polar​​molecule​​due​​to​​uneven​​distribution​​of​​charge​​within​​molecule​​(creates​​a​​dipole)​
​-​ ​O​2​ ​ ​attracts​​electrons​​more​​strongly​​than​​H​+​ ​ ​atoms​​(O​​2​ ​is​​more​
​electronegative)​
​-​ ​Unequal​​sharing​​of​​electrons​​gives​​water​​a​​slightly​​negative​​charge​​near​​the​​O​2​ ​ ​atom​
​and​​slightly​​positive​​charge​​near​​H​+​ ​ ​atom​
​-​ ​Water​​forms​​hydrogen​​bonds​​with​​each​​other​

​Water​​is​​a​​metabolite​​/​​reagent​​:​
​-​ ​Its​​a​​metabolite​​/​​reagent​​in​​metabolic​​reactions​​such​​as​​condensation​​and​​hydrolysis​

​Water​​is​​a​​solvent​​:​
​-​ ​Good​​solvent​​(Many​​metabolic​​reactions​​occur​​in),​​dissolves​​ions​​&​​polar​​molecules​​(E.g,​​salts​​and​​glucose)​
​-​ ​Enables​​transports​​of​​solutes​​in​​organisms​
​-​ ​Non-polar​​molecules​​like​​fats​​don’t​​dissolve​​well​​as​​they​​are​​hydrophobic​

​Water​​has​​a​​high​​specific​​heat​​capacity​​:​
​-​ ​Requires​​a​​lot​​of​​energy​​to​​warm​​(Due​​to​​hydrogen​​bonds​​which​​absorb​​heat​​energy)​
​-​ ​Minimises​​temperature​​fluctuations​​in​​living​​things​​therefore​​it​​acts​​as​​a​​buffer​
​-​ ​This​​is​​good​​for​​:​​Stable​​aquatic​​environments,​​Maintaining​​internal​​body​​temp​​for​​enzyme​​function,​​Distribution​​of​​heat​​via​​blood​​and​
​tissue​​fluid​

​Water​​has​​a​​high​​latent​​heat​​of​​vaporisation​​:​
​-​ ​Requires​​a​​lot​​of​​energy​​to​​evaporate​​water​​(brake​​hydrogen​​bonds)​
​-​ ​Evaporation​​of​​water​​provides​​cooling​​effect​​with​​little​​water​​loss​

​Cohesion​​:​
​-​ ​Molecules​​stick​​to​​each​​other​​via​​hydrogen​​bonds​
​-​ ​Helps​​water​​to​​move​​continuously​​in​​columbs​​(E.g​​xylem,​​blood​​vessels)​

​Adhesion​​:​
​-​ ​Water​​sticks​​to​​other​​substances​​(E.g,​​cellulose​​in​​plant​​walls​​helping​​with​​capillary​​action​​(movement​​up​​xylem))​

​Density​​:​
​-​ ​Ice​​is​​less​​dense​​than​​water​​due​​to​​the​​spacing​​of​​hydrogen​​bonds​
​-​ ​Ice​​floats​​insulating​​water​​below​​and​​allowing​​aquatic​​life​​to​​survive​​in​​cold​​habitats​

​Monomers​​and​​polymers​​:​
​ onomers​​:​​Small​​units,​​small​​simple​​molecules​​(E.g,​​include​​monosaccharide​​glucose,​​amino​​acids​​&​​nucleotides)​
M
​Polymers​​:​​Molecules​​made​​from​​monomers​​joined​​together,​​Process​​of​​joining​​monomers​​is​​called​​polymerization​
​Macromolecules​​:​​Very​​large​​molecules,​​May​​or​​may​​not​​be​​polymers,​​All​​molecules​​are​​macromolecules,​​but​​not​​all​​macromolecules​​are​
​polymers​

​Condensation​​reaction​​:​
​-​ ​Joins​​monomers​​by​​covalent​​bonds​
​-​ ​Removes​​a​​molecule​​of​​water​
​-​ ​Forms​​polymers​​or​​macromolecules​

​Hydrolysis​​reaction​​:​
​-​ ​Breaks​​covalent​​bonds​​in​​polymers​
​-​ ​Water​​is​​added​​to​​break​​bonds​

​Carbohydrates​​:​
-​ ​ ​Consists​​of​​only​​carbon,​​hydrogen​​and​​oxygen​
​-​ ​Long​​chains​​of​​sugar​​units​​called​​saccharides​
​Three​​types​​of​​saccharides​​:​​Monosaccharides​​can​​join​​to​​form​​disaccharides​​and​​polysaccharides​​by​​glycosidic​​bonds​​formed​​in​
​condensation​​reactions.​
​Monosaccharides​​:​
​Glucose​​is​​a​​monosaccharide​​:​
​-​ ​Contains​​6​​carbon​​atoms​​in​​each​​molecule​
​-​ ​Main​​substrate​​for​​respiration​
​-​ ​Has​​two​​isomers,​​beta​​and​​alpha​​glucose​​→​

​Disaccharides​​:​
​ ​​Glucose​​+​​Glucose​​→​​Maltose​​+​​Water​
α
​α​​Glucose​​+​​Galactose​​→​​Lactose​​+​​Water​
​β​​Glucose​​+​​Fructose​​→​​Sucrose​​+​​Water​

​Polysaccharides​​are​​formed​​from​​many​​glucose​​units​​joined​​together​​and​​include​​:​
​-​ ​Glycogen​​and​​starch​​←​​Both​​formed​​from​​condensation​​of​​alpha​​glucose​
​-​ ​Cellulose​​←​​Formed​​from​​condensation​​of​​beta​​glucose​

​1,6​​glycosidic​​bonds​​result​​in​​branching​

​Glycogen​​:​
​-​ ​Main​​energy​​storage​​molecule​
​-​ ​Formed​​from​​many​​alpha​​glucose​​molecules​​joined​​by​​1,4​​and​​1,6​​glycosidic​​bonds​
∴
​-​ ​Has​​large​​number​​of​​side​​branches​​so​​glucose​​&​​ ​​energy​​can​​be​​released​​quickly​
∴
​-​ ​Relatively​​large​​but​​compact​​ ​​maximising​​amount​​of​​energy​​it​​can​​store​
​-​ ​Insoluble​​due​​to​​large​​size​​-​​Don’t​​affect​​water​​potential​​of​​cells,​​prevent​​osmosis​​water​​uptake,​​unlike​​glucose,​
​which​​would​​draw​​water​​into​​cells​

​Starch​​:​
​-​ ​Store​​of​​energy​​in​​plants​
​-​ ​Mixture​​of​​two​​polysaccharides​​←​​Amylose​​and​​amylopectin​
​-​ ​Amylose​​:​​Unbranched​​chain​​of​​glucose​​molecules​​joined​​by​​1,4​​glycosidic​​bonds​​←coiled​​and​​ ​​very​ ∴
​compact​​molecule​​so​​can​​store​​a​​lot​​of​​energy​
​-​ ​Amylopectin​​:​​Branched,​​made​​of​​glucose​​molecules​​joined​​by​​1,4​​and​​1,6​​glycosidic​​bonds,​​due​​to​
∴
​presence​​of​​many​​side​​branches,​​it​​is​​rapidly​​digested​​by​​enzymes​​ ​​energy​​is​​released​​quickly​
​-​ ​Insoluble​​due​​to​​large​​size​​-​​Don’t​​affect​​water​​potential​​of​​cells,​​prevent​​osmosis​​water​​uptake,​​unlike​
​glucose,​​which​​would​​draw​​water​​into​​cells​

​Cellulose​​:​
​-​ ​Component​​of​​the​​cell​​wall​​in​​plants​
​-​ ​Composed​​of​​long,​​unbranched​​chains​​of​​beta​​glucose​​joined​​by​​1,4​​glycosidic​​bonds​
​-​ ​Microfibrils​​are​​strong​​threads​​made​​of​​long​​cellulose​​chains​​joined​​by​​hydrogen​​bonds​
​-​ ​Provide​​structural​​support​​in​​plant​​cells​

​Lipids​​:​
​Molecules​​which​​are​​only​​soluble​​in​​organic​​solvents​​(E.g​​alcohols)​

​Two​​types​​of​​lipids​​(specifically​​fatty​​acids)​​:​
​Saturated​​:​
-​ ​ ​ aturated​​fatty​​acid​​(Saturated​​lipid)​​found​​in​​animal​​fats​
S
​-​ ​Don’t​​contain​​any​​carbon-carbon​​double​​bonds​

​Unsaturated​​:​
-​ ​ ​ nsaturated​​fatty​​acid​​(Unsaturated​​lipid)​​found​​in​​plants​
U
​-​ ​Contains​​carbon-carbon​​double​​bonds​
​-​ ​Melt​​at​​a​​lower​​temperature​​the​​saturated​​fats​

​ he​​greater​​number​​of​​unsaturated​​bonds,​​the​​weaker​​the​​intermolecular​​bonds​​resulting​​in​​a​​lower​​melting​​point.​
T
∴
​ ​​Saturated​​fats​​are​​solid​​at​​room​​temp​​and​​Unsaturated​​fats​​are​​liquid​​at​​room​​temp​
​Triglycerides​​(fats​​and​​oils)​​:​
-​ ​ ​ ipids​​made​​of​​one​​molecule​​of​​glycerol​​and​​three​​fatty​​acids​
L
​-​ ​Joined​​by​​ester​​bonds​
​-​ ​Formed​​in​​condensation​​reactions​
​-​ ​There​​are​​many​​different​​types​​of​​fatty​​acid​
​-​ ​They​​vary​​in​​chain​​length,​​presence​​and​​number​​of​​double​​bond​
-​ ​ ​Some​​triglycerides​​contain​​a​​mix​​of​​different​​fatty​​acids​
​-​ ​Triglycerides​​are​​used​​as​​energy​​reserves​​in​​plant​​and​​animal​​cells​

​Phospholipids​​:​
-​ ​ ​ ne​​of​​the​​fatty​​acids​​of​​a​​triglyceride​​is​​substituted​​by​​a​​phosphate​​group​
O
​-​ ​Phosphate​​heads​​are​​hydrophilic​​and​​the​​tails​​are​​hydrophobic​
​-​ ​As​​a​​result​​phospholipids​​form​​micelles​​when​​they​​are​​in​​contact​​with​
​water​
​-​ ​Heads​​are​​on​​the​​outside​​as​​they​​are​​attracted​​to​​water​​and​​tails​​are​​on​
​the​​inside​​as​​they​​move​​away​​from​​water.​

​Inorganic​​ions​​:​
​ ccur​​in​​solution​​in​​the​​cytoplasm​​and​​body​​fluid​​of​​organisms,​​some​​high​​in​​concentrations​​and​​others​​in​​very​​low​
O
​concentrations.​

​ ydrogen​​ions​​(H​​+​​)​​:​​Determine​​pH​​of​​substances​​such​​as​​blood,​​The​​higher​​the​​concentration​​of​​H​+​ ​ ​the​​lower​​the​​pH​
H
​Calcium​​ions​​(Ca​​2+​​)​​:​​Involved​​in​​muscle​​contraction,​​Synaptic​​transmission,​​Blood​​clotting,​​Enzyme​​cofactor​
​Iron​​ions​​(Fe​​2+​​/​​Fe​​3+​​)​​:​​Component​​of​​haemoglobin​​which​​is​​an​​oxygen​​carrying​​molecule​​in​​RBCs​
​Sodium​​ions​​(Na​​+​​)​​:​​Involved​​in​​co-transport​​of​​glucose​​and​​amino​​acids​
​Phosphate​​ions​​:​​Component​​of​​DNA​​and​​ATP​

​Proteins​​:​

​Amino​​Acids​​:​
-​ ​ ​ he​​monomers​​proteins​​are​​made​​of​
T
​-​ ​Amino​​acids​​contain​​an​​amino​​group,​​carboxylic​​group​​and​​a​​variable​​R​​group​​(with​​20​
​different​​variations)​
-​ ​ ​Amino​​acids​​are​​joined​​by​​peptide​​bonds​​formed​​in​​condensation​​reactions.​
​-​ ​A​​dipeptide​​contains​​two​​amino​​acids​
​-​ ​Polypeptides​​contain​​three​​or​​more​​amino​​acids​

​Structure​​of​​proteins​​:​
​Determined​​by​​order​​and​​number​​of​​amino​​acids,​​bonding​​present​​and​​the​​shape​​of​​protein​

​Primary​​structure​​:​
​-​ ​Order​​and​​number​​of​​amino​​acids​​present​​in​​the​​protein​

​Secondary​​structure​​:​
-​ ​ ​ hape​​that​​the​​chain​​of​​amino​​acids​​take​
S
​-​ ​Either​​alpha​​helix​​or​​beta​​pleated​​sheet​
​-​ ​Shape​​is​​determined​​by​​hydrogen​​bonding​

​Tertiary​​structure​​:​
​-​ ​3D​​shape​​of​​the​​protein​
​-​ ​Can​​be​​globular​​or​​fibrous​
​-​ ​Globular​​proteins​​(E.g,​​enzymes)​​are​​compact​
​-​ ​FIbrous​​proteins​​(E.g,​​keratin)​​are​​long​​and​​can​​be​​used​​to​​form​​fibres​

​Quaternary​​structure​​:​
​-​ ​Combination​​of​​2​​or​​more​​polypeptide​​chains​​into​​a​​functional​​protein​
​Collagen​​(Fibrous​​protein)​​:​
​-​ ​Very​​strong​​due​​to​​presence​​of​​both​​hydrogen​​and​​covalent​​bond​
​-​ ​The​​molecules​​wrap​​around​​each​​other​​and​​form​​fibrils​​which​​form​​strong​​collagen​​fibres​
​-​ ​Forms​​the​​structure​​of​​bones,​​cartilage​​and​​connective​​tissues​
​-​ ​Is​​main​​component​​of​​tendons​

​Hemoglobin​​(Globular​​protein)​​:​
​-​ ​Water​​soluble​
​-​ ​Consists​​of​​two​​alpha​​and​​two​​beta​​polypeptide​​chains,​​each​​containing​​a​​haem​​group​
​-​ ​Carries​​O​​2​ ​in​​the​​blood​​as​​O​​2​ ​binds​​to​​the​​haem​​(Fe​​2+​​)​​group​​and​​O​​2​ ​is​​released​​when​​required​

​Biochemical​​tests​​:​

​Benedicts​​test​​:​
​-​ ​Tests​​for​​reducing​​and​​non-reducing​​sugars​
​-​ ​Reducing​​sugar​​is​​one​​which​​can​​donate​​electrons​​(Includes​​all​​monosaccharides​​and​​some​​disaccharides)​
​-​ ​An​​alkaline​​solution​​of​​blue​​copper​​(II)​​sulphate​​is​​added​​to​​the​​sugar​​and​​heated​
​-​ ​In​​presence​​of​​reducing​​sugar​​a​​red​​precipitate​​is​​formed​
​-​ ​Following​​a​​negative​​test​​:​
​-​ ​Add​​hydrochloric​​acid​​and​​heat​​(Sodium​​hydrolysis)​
​-​ ​Cool​​solution​​and​​add​​an​​alkali​​(Sodium​​hydroxide)​​to​​neutralise​
​-​ ​Add​​Benedict's​​solution​​and​​heat​​for​​5​​mins​​at​​80​​o​C​
​
​-​ ​If​​there​​is​​a​​non-reducing​​sugar​​solution​​will​​go​​from​​blue​​to​​green​​,​​yellow​​,​​orange​​or​​brick​​red​

​Biuret​​test​​:​
-​ ​ ​ ests​​for​​proteins​
T
​-​ ​Place​​sample​​solution​​in​​test​​tube​
​-​ ​Add​​as​​equal​​amount​​of​​NaOH​
​-​ ​Add​​a​​few​​drops​​of​​dilute​​copper​​(II)​​sulfate​​solution​​and​​gently​​mix​
​-​ ​In​​the​​presence​​of​​a​​protein​​the​​solution​​goes​​from​​blue​​to​​lilac​
​-​ ​An​​indicator​​of​ ​peptide​​bonds​
​-​ ​If​​there​​is​​no​​protein​​solution​​remains​​blue​

​Emulsion​​test​​:​
-​ ​ ​ ests​​for​​lipids​
T
​-​ ​Add​​2​​ml​​of​​sample​​to​​5​​ml​​of​​cold​​ethanol​​and​​mix​​thoroughly​
​-​ ​Add​​5​​ml​​of​​water​​and​​mix​
​-​ ​In​​presence​​of​​lipids​​solution​​goes​​cloudy​
​-​ ​Due​​to​​formation​​of​​an​​emulsion​​where​​the​​light​​is​​refracted​​as​​it​​passes​​from​​droplets​​of​​oil​​to​​water​

​Iodine​​test​​:​
-​ ​ ​ ests​​for​​starch​
T
​-​ ​Add​​iodine​​(Potassium​​iodide)​​to​​sample​
​-​ ​In​​presence​​of​​starch​​goes​​from​​yellow​​to​​blue​​/​black​

​Nucleotides​​and​​nucleic​​acids​​:​
​Nucleotides​​:​​Monomers​​from​​which​​DNA​​and​​RNA​​polymers​​are​​built​

​DNA​​nucleotide​ ​RNA​​nucleotide​

​Pentose​​sugar​ ​Deoxyribose​ ​Ribose​

​Bases​​involved​ ​Adenine​​(A)​​-​​Thymine​​(T)​ ​Adenine​​(A)​​-​​Uracil​​(U)​

​-​ ​(2​​hydrogen​​bonds)​ ​-​ ​(2​​hydrogen​​bonds)​
​Guanine​​(G)​​-​​Cytosine​​(C)​ ​Guanine​​(G)​​-​​Cytosine​​(C)​
​-​ ​(3​​hydrogen​​bonds)​ ​-​ ​(3​​hydrogen​​bonds)​

​Number​​of​​strands​ ​Double-stranded​​helix​ ​Single-stranded​​(relatively​​short)​

 ​Overall​​structure​

​Purines​​and​​Pyrimidines​​:​ ​Phosphodiester​​bonds​​:​

​-​ ​ NA​​and​​RNA​​are​​polynucleotides​​(Long​​chains​​of​
D
​nucleotides)​
​-​ ​Nucleotides​​join​​via​​condensation​​reactions​
​-​ ​Between​​the​​phosphate​​of​​one​​nucleotide​​and​​the​
​sugar​​of​​the​​next​
​-​ ​This​​forms​​a​​phosphodiester​​bond​
​-​ ​Name​​for​​involving​​a​​phosphate​​&​​two​​ester​
​bonds​
​-​ ​Multiple​​of​​these​​bonds​​create​​the​
​sugar-phosphate​​backbones​

​ATP​​:​
​-​ ​Adenosine​​triphosphate​
​-​ ​Consists​​of​​ribose,​​adenine​​and​​3​​phosphate​​groups​
-​ ​ ​Universal​​energy​​currency​​used​​by​​all​​living​​cells​
​-​ ​Energy​​is​​released​​when​​ATP​​is​​hydrolyzed​​(catalysed​​by​​ATP​ ​hydrolase)​
​-​ ​Forms​​ADP​​+​​PI​​(Inorganic​​phosphate)​
-​ ​ ​The​​inorganic​​phosphate​​can​​be​​used​​to​​phosphorylate​​other​​compounds​​←​​making​​them​​more​​reactive​
​-​ ​Condensation​​of​​ADP​​and​​inorganic​​phosphate​​catalysed​​by​​ATP​​synthase​​produces​​ATP​​during​​photosynthesis​​and​​respiration​

​DNA​​replication​​:​

​Semi-conservative​​replication​​of​​DNA​​:​
​ eading​​strand​​:​​5’​​-​​3’​​(continuous​​replication)​
L
​Lagging​​strand​​:​​3’​​-​​5’​​(discontinuous​​replication)​

​Purpose​​:​
​-​ ​DNA​​must​​be​​copied​​before​​cell​​division​​to​​ensure​​each​​daughter​​cell​​receives​​a​​full​
​genetic​​set​
​-​ ​This​​is​​done​​by​​semi-conservative​​replication,​​where​​:​
​-​ ​One​​strand​​from​​the​​original​​DNA​​is​​conserved​
​-​ ​One​​strand​​is​​newly​​synthesized​

​Replication​​process​​:​
​1.​ ​DNA​​gyrase​​unwinds​​the​​double​​helix​
​2.​ ​DNA​​helicase​​breaks​​hydrogen​​bonds​​between​​the​​base​​pairs​
​3.​ ​Free​​activated​​nucleotides​​bind​​to​​exposed​​complementary​​bases​​on​​both​​template​
​strands​
​4.​ ​DNA​​polymerase​​:​
​-​ ​Catalyses​​condensation​​reactions​
 ​-​
​ orms​​phosphodiester​​bonds​​between​​adjacent​​nucleotides,​​creating​​the​
F
​new​​sugar-phosphate​​backbone​
​5.​ ​Hydrogen​​bonds​​form​​between​​complementary​​base​​pairs,​​restoring​​the​​double​
​helix​

​Why​​one​​strand​​is​​conserved​​:​
​-​ ​Ensure​​accuracy​​:​​each​​new​​strand​​is​​built​​against​​a​​correct​​template​
​-​ ​Maintains​​genetic​​continuity​​across​​generations​​of​​cells​
​-​ ​Vital​​for​​new​​cells​​to​​function​​like​​parent​​cells​

​Spontaneous​​mutations​​:​
​-​ ​Though​​highly​​accurate,​​random​​replication​​errors​​can​​occur​​:​
​-​ ​Wrong​​base​​added​
​-​ ​Extra​​base​​inserted​
​-​ ​Base​​missed​​entirely​
​-​ ​These​​spontaneous​​mutations​​can​​alter​​the​​DNA​​sequence​

​The​​genetic​​code​​:​
-​ ​ ​ he​​order​​of​​bases​​on​​DNA​​is​​called​​the​​genetic​​code​​which​​consists​​of​​triplet​​bases​
T
​-​ ​Codon​​:​​Each​​triplet​​of​​bases​​that​​codes​​for​​a​​particular​​amino​​acids​
​-​ ​The​​amino​​acids​​are​​joined​​together​​by​​peptide​​bonds​​and​​form​​a​​polypeptide​​chain​

​A​​gene​​is​​a​​sequence​​of​​bases​​on​​a​​DNA​​molecule​​coding​​for​​a​​sequence​​of​​amino​​acids​​in​​a​​polypeptide​​chain.​
​-​ ​Not​​all​​the​​gene​​codes​​for​​proteins​
​-​ ​Non-coding​​sections​​of​​DNA​​are​​called​​introns​
​-​ ​Coding​​regions​​of​​DNA​​are​​called​​exons​

​Features​​of​​the​​genetic​​code​​:​
​-​ ​Genetic​​code​​is​​non-overlapping​
​-​ ​Each​​triplet​​is​​only​​read​​once​​and​​triplets​​don’t​​share​​any​​bases​
​-​ ​Genetic​​code​​is​​degenerate​
​-​ ​More​​than​​one​​triplet​​codes​​for​​the​​same​​amino​​acid​
​-​ ​Reduced​​the​​phenotypic​​effect​​of​​mutations​​(which​​are​​mistakes​​in​​the​​base​​sequence​​such​​as​​base​​deletion,​​insertion​​or​
​substitution)​
∴
​-​ ​A​​change​​in​​the​​base​​sequence​​of​​DNA​​may​​alter​​the​​amino​​acid​​sequence​​and​​the​​protein​​ ​​it​​can​​have​​various​​effects​
​-​ ​Some​​mutations​​are​​harmful​​(E.g,​​mutation​​leading​​to​​production​​of​​sticky​​mucus​​&​​causes​​cystic​​fibrosis​​or​​sickle​
​cell​​anaemia)​
​-​ ​The​​genetic​​code​​contains​​start​​and​​stop​​codons​​which​​either​​start​​or​​stop​​protein​​synthesis​

​Protein​​synthesis​​:​
​There​​are​​two​​stages​​of​​protein​​synthesis​​:​
​-​ ​Transcription​​:​​Occurs​​in​​the​​nucleus​​and​​involves​​DNA​​and​​mRNA​
​-​ ​The​​DNA​​strand​​is​​transcribed​​into​​mRNA​
​-​ ​Translation​​:​ ​Involves​​mRNA,​​tRNA​​and​​ribosomes​
​-​ ​The​​process​​during​​which​​the​​amino​​acids​​are​​assembled​​together​​to​​form​​a​
​polypeptide​​chain​​/​​protein​

​Transcription​​:​
​A​​molecule​​of​​mRNA​​is​​made​​in​​the​​nucleus​​:​
​-​ ​DNA​​unwinds​​(DNA​​gyrase)​​←​​Hydrogen​​bonds​​between​​base​​pairs​​break​​(DNA​
∴
​helicase)​​ ​​separating​​the​​two​​strands​
​-​ ​One​​of​​the​​DNA​​strands​​is​​used​​as​​a​​template​​by​​RNA​​polymerase​​to​​make​​the​
​mRNA​​molecule.​​The​​DNA​​template​​is​​called​​the​​antisense​​strand​
​-​ ​Free​​RNA​​nucleotides​​line​​up​​by​​complementary​​base​​pairing​​and​​adjacent​
∴
​nucleotides​​are​​joined​​by​​phosphodiester​​bonds​​made​​by​​RNA​​polymerase​​ ​​forming​
​a​​single​​stranded​​molecule​​of​​mRNA​
​-​ ​mRNA​​then​​moves​​out​​of​​the​​nucleus​​through​​a​​pore​​and​​attaches​​to​​a​​ribosome​​in​
​the​​cytoplasm​​which​​is​​the​​site​​of​​the​​next​​stage​​of​​protein​​synthesis​​(translation)​

​Translation​​:​
​Amino​​acids​​join​​together​​to​​form​​a​​polypeptide​​chain​
​-​ ​mRNA​​attaches​​to​​a​​ribosome​​and​​the​​transfer​​RNA​​collects​​amino​​acids​​from​​the​
​cytoplasm​​and​​carries​​them​​to​​the​​ribosome.​
∴
​-​ ​tRNA​​is​​a​​single​​stranded​​molecule​​with​​a​​binding​​site​​at​​one​​end​​ ​​it​​can​
​only​​carry​​one​​type​​of​​amino​​acid,​​and​​a​​triplet​​of​​bases​​at​​the​​other​
 -​ ​ t​RNA​​attaches​​itself​​to​​mRNA​​by​​complementary​​base​​pairing​​←​​two​​molecules​​attach​​to​​mRNA​​at​​a​​time​
​-​ ​The​​amino​​acids​​attached​​to​​two​​tRNA​​molecules​​join​​by​​a​​peptide​​bond​​and​​then​​tRNA​​molecules​​detach​​themselves​​from​​the​
​amino​​acids,​​leaving​​them​​behind​
​-​ ∴
​This​​process​​is​​repeated​​ ​​leading​​to​​the​​formation​​of​​a​​polypeptide​​chain​​until​​a​​stop​​codon​​is​​reached​​on​​mRNA​​and​​ends​​the​
​process​​of​​protein​​synthesis​

​Enzymes​​:​
-​ ​ ​ iological​​catalysts​
B
​-​ ​Made​​of​​globular​​proteins​​and​​are​​made​​inside​​cells​​through​​protein​​synthesis​
​-​ ​Essential​​for​​controlling​​nearly​​all​​metabolic​​reactions​
​-​ ​Increase​​the​​rate​​of​​reaction​​by​​lowering​​the​​activation​​energy​​of​​the​​reaction​​they​​catalyse​
​-​ ​The​​active​​site​​is​​the​​area​​of​​an​​enzyme​​where​​the​​reaction​​with​​the​​substrate​​takes​​place​
​-​ ∴
​Enzymes​​are​​specific​​to​​substrates​​they​​bind​​to​​ ​​only​​one​​type​​of​​substrate​​fits​​into​​the​​active​​site​​of​​an​​enzyme​

​Enzyme​​models​​:​

​Lock​​-​​and​​-​​key​​theory​​:​
-​ ​ ​ nzyme​​and​​substrate​​fit​​exactly​
E
​-​ ​No​​structural​​change​​during​​binding​

​Induced​​fit​​model​​:​
​-​ ​ hen​​the​​enzyme​​and​​substrate​​form​​a​​complex,​
W
​the​​structure​​of​​the​​enzyme​​is​​altered​​so​​that​​the​​active​​site​​of​​the​​enzyme​​fits​​around​​the​​substrate​

​Intracellular​​and​​extracellular​​enzymes​​:​
I​ntracellular​​enzymes​​-​​Work​​inside​​the​​cell​
​Extracellular​​enzymes​​-​​Secreted​​and​​work​​outside​​the​​cell​

​Intracellular​ ​Extracellular​

​Example​ ​Catalase​ ​Amylase​

​Function​​of​​enzyme​ ​-​ ​ rotects​​cells​​from​​oxidative​

P ​-​ ​ reaks​​down​​complex​
B
​damage​​by​​catalyzing​​the​ ​carbohydrates,​​into​​similar​​sugars​
​decomposition​​of​​hydrogen​ ​which​​the​​body​​can​​then​​absorb​
​peroxide​​into​​water​​and​​oxygen​ ​and​​use​​for​​energy​

​Factors​​affecting​​rate​​of​​enzyme​​controlled​​reactions​​:​

​Enzyme​​concentration​​:​
​-​ ​The​​rate​​of​​reaction​​increases​​as​​enzyme​​concentration​​increases​
​-​ ​This​​is​​because​​there​​are​​more​​active​​sites​​for​​substrates​​to​​bind​​to​
​-​ ​However,​​beyond​​a​​certain​​point​​the​​rate​​of​​reaction​​as​​there​​are​​more​​active​​sites​​than​​substrates​
​-​ ​So​​substrate​​concentration​​becomes​​limiting​​factor​

​Substrate​​concentration​​:​
​-​ ​Rate​​of​​reaction​​increases​​as​​substrate​​concentration​​increases​
​-​ ​This​​is​​because​​more​​enzyme-substrate​​complexes​​are​​formed​
​-​ ​However,​​beyond​​a​​certain​​point​​the​​rate​​of​​reaction​​no​​longer​​increases​​there​​are​​more​​substrates​​than​​active​​sites​
​-​ ​Enzyme​​concentration​​in​​the​​limiting​​factor​

​Temperature​​:​
​-​ ​Rate​​of​​reaction​​increases​​up​​to​​the​​optimum​​temperature​
​-​ ​Temperature​​which​​enzymes​​work​​at​​their​​maximum​​rate​
​-​ ​Rate​​of​​reaction​​decreases​​above​​the​​optimum​​temperature​
​-​ ​Enzymes​​begin​​to​​denature​

​pH​​:​
​-​ ​Rate​​of​​reaction​​increases​​up​​to​​the​​optimum​​pH​
​-​ ​pH​​which​​enzymes​​work​​at​​their​​maximum​​rate​
​-​ ​Rate​​of​​reaction​​decreases​​above​​optimum​​pH​
​-​ ​Enzymes​​begin​​to​​denature​
​Denaturing​​of​​enzymes​​:​
-​ ​ ∴
​ igh​​temperature​​ ​​enzymes​​vibrate​​more​
H
​-​ ​Hydrogen​​+​​ionic​​bonds,​​holding​​enzymes​​tertiary​​structure,​​break​
​-​ ∴ ∴
​Active​​site​​changes​​ ​​substrate​​no​​longer​​fits​​ ​​enzyme-substrate​​complex​​can’t​​form​
​-​ ​Denaturation​​is​​irreversible​

​Inhibitors​​:​
-​ ​ ​ ubstance​​which​​slows​​down​​or​​stops​​a​​reaction​​by​​affecting​​the​​binding​​of​​substrate​​to​​the​​enzyme​
S
​-​ ​Inhibitors​​can​​either​​be​​reversible​​or​​irreversible​
​-​ ​Examples​​of​​irreversible​​inhibitors​​:​
∴
​-​ ​Heavy​​metal​​ions,​​such​​as​​mercury​​and​​silver,​​which​​cause​​disulphide​​bonds​​within​​the​​protein​​structure​​to​​break​​ ​​causing​
∴
​the​​shape​​of​​the​​active​​site​​to​​change​​ ​​affecting​​protein​​activity​
∴
​-​ ​Cyanide,​​which​​is​​a​​nerve​​gas​​that​​covalently​​binds​​to​​the​​active​​site,​​ ​​preventing​​the​​binding​​of​​the​​substrate​​of​​oxygen​
​and​​ATP​
-​ ​ ∴
​Reversible​​inhibitors​​bind​​to​​the​​active​​site​​through​​hydrogen​​bonds​​and​​weak​​ionic​​interactions​​ ​​don’t​​bind​​permanently​
​-​ ​Reversible​​inhibitors​​can​​be​​either​​competitive​​or​​non-competitive​

​Competitive​​inhibitors​​:​
-​ ​ ∴
​ imilar​​in​​structure​​to​​the​​substrate​​ ​​bind​​to​​the​​active​​site​​of​​the​​enzyme​
S
​-​ ​Decreases​​enzyme​​activity​​as​​they​​compete​​with​​substrate​​for​​the​​enzyme​
​-​ ​The​​amount​​of​​product​​formed​​remains​​the​​same,​​however​​the​​rate​
​decreases​
​-​ ​The​​higher​​the​​concentration​​of​​competitive​​inhibitor​​the​​lower​​the​​rate​​of​
​reaction​
​-​ ​Increasing​​the​​substrate​​concentration​​reverses​​effect​​of​​competitive​
​inhibitor​​by​​outcompeting​​them​

​Non-competitive​​inhibitors​​:​
​-​ ​ on’t​​bind​​to​​the​​active​​site,​​instead​​they​​bind​​to​​another​​site​​on​​the​​enzyme​
D
​called​​the​​allosteric​​site​
​-​ ​Binding​​of​​the​​non-competitive​​inhibitor​​changes​​the​​shape​​of​​the​​active​​site​
∴ ​ ​​preventing​​the​​binding​​of​​the​​substrate​
​-​ ​Increasing​​the​​concentration​​of​​substrate​​has​​no​​effect​​on​​non-competitive​
​inhibition​

​Cofactors,​​Coenzymes,​​Activators​​and​​Prosthetic​​groups​​:​

​Cofactors​​:​
-​ ​ ​ ​​cofactor​​is​​a​​non-protein​​compound​​required​​for​​an​​enzyme’s​​activity​​to​​occur​
A
​-​ ​There​​are​​three​​types​​of​​cofactors​​:​
​-​ ​Coenzymes​
​-​ ​Activators​
​-​ ​Prosthetic​​groups​

​Coenzymes​​:​
-​ ​ ​ rganic​​cofactors​​which​​don’t​​permanently​​bind​
O
​-​ ​They​​facilitate​​the​​binding​​of​​substrate​​to​​enzyme​
​-​ ​Many​​coenzymes​​are​​vitamin​​derived​
​-​ ​E.g,​​NAD,​​derived​​from​​B​​vitamins,​​acts​​as​​a​​hydrogen​​acceptor​

​Activators​​:​
​-​ ​Inorganic​​metal​​ions​​which​​temporarily​​bind​​to​​the​​enzyme​​and​​alters​​its​​active​​site​​making​​the​​reaction​​more​​feasible​
​-​ ​E.g,​​Magnesium​​ion​​is​​an​​important​​activator​​involved​​in​​processes​​such​​as​​shielding​​negative​​charge​

​Prosthetic​​groups​​:​
​-​ ​Permanently​​attached​​to​​the​​enzyme​
​-​ ​E.g,​​hemoglobin​​contains​​a​​prosthetic​​haem​​group​​which​​contains​​iron,​​permanently​​bound​​to​​the​​molecule​​which​​serves​​as​
​a​​means​​of​​binding​​oxygen​

​Biological​​membranes​​:​
​ ll​​cells​​and​​organelles​​are​​surrounded​​by​​the​​partially​​permeable​​membrane​
A
​Cell​​surface​​membrane​​:​​Separates​​internal​​and​​external​​environment​
​-​ ​Partially​​permeable​​:​​Controls​​the​​movement​​of​​substances​​in​​and​​out​​of​​cells​​and​​organelles​
​-​ ​Contains​​receptors​​:​​Has​​receptors​​for​​other​​molecules​​such​​as​​hormones​​and​​enables​​adjacent​​cells​​to​​stick​​together​
​Fluid​​mosaic​​model​​:​
​-​ ​ alled​​this​​due​​to​​the​​membranes​​fluidity​​and​​mosaic​​like​
C
​structure​​(random​​distribution​​of​​proteins)​

​Components​​:​
​Phospholipids​​:​
​-​ ​Form​​the​​bilayer​​-​​hydrophilic​​heads​​outside,​​hydrophobic​
​tails​​inside​
​-​ ​Barrier​​to​​water-soluble​​substances​​(E.g,​​ions,​​sugars)​
​-​ ​Can​​act​​as​​signalling​​molecules​​if​​modified​​or​​hydrolyzed​

​Cholesterol​​:​
​-​ ​Regulates​​fluidity​​:​
​-​ ​Prevents​​rigidity​​at​​low​​temperatures​
​-​ ​Prevents​​excess​​fluidity​​at​​high​​temperatures​
​-​ ​Adds​​stability​​and​​mechanical​​strength​
​-​ ​Reduces​​permeability​

​Glycoproteins​​and​​Glycolipids​​:​
​-​ ​Involved​​in​​:​
​-​ ​Cell​​signalling​
​-​ ​Endocytosis​
​-​ ​Cell​​adhesion​​and​​recognition​
​-​ ​Reduces​​permeability​

​Transport​​proteins​​:​
​-​ ​Provide​​hydrophilic​​channels​​for​​ions​​/​​polar​​molecules.​
​-​ ​Channel​​proteins​​:​ ​allow​​passive​​movement​
​-​ ​Carrier​​proteins​​:​​Change​​shape​​to​​transport​​molecules.​
​-​ ​Highly​​specific​​←​​Control​​substance​​entry​​/​​exit.​

​Permeability​​:​
​-​ ​As​​temperature​​increases​​membrane​​permeability​​increases​

​High​​temperatures​​:​
∴ ∴
​-​ ​Phospholipids​​gain​​kinetic​​energy​​ ​​move​​more​​ ​​becomes​​loosely​​packed​
​-​ ​Membranes​​become​​more​​fluid​​and​​less​​stable​
​-​ ​Extreme​​heat​​may​​cause​​the​​bilayer​​to​​melt​​/​​disintegrate​
∴ ∴
​-​ ​Proteins​​(Channel​​/​​carrier)​​denature​​ ​​loses​​shape​​and​​function​​ ​​uncontrolled​​transport​

​Low​​temperatures​​:​
∴
​-​ ​Ice​​crystals​​may​​form​​ ​​pierce​​the​​membrane,​​increasing​​permeability​
​-​ ​Upon​​thawing,​​proteins​​may​​still​​be​​deformed,​​affecting​​control​​of​​transport​

​Water​​expansion​​:​
∴
​-​ ​Heated​​water​​inside​​the​​cell​​expands,​​increasing​​pressure​​ ​​membrane​​stress​​and​​protein​​deformation​

​Transport​​mechanisms​​:​
​-​ ​Type​​of​​mechanism​​depends​​on​​the​​properties​​of​​the​​molecule​​and​​the​​requirements​​of​​the​​cell​

​Diffusion​​:​
​-​ ​Passive​​movement​​of​​small,​​non-polar​​lipid​​soluble​​molecules​​(E.g,​​CO​​2​ ​and​​O​​2​)​ ​
​-​ ​Moves​​from​​an​​area​​of​​high​​concentration​​to​​an​​area​​of​​low​​concentration​​(Goes​​down​​the​
​concentration​​gradient)​
​-​ ​The​​molecules​​move​​directly​​through​​the​​phospholipid​​bilayer​
​-​ ​Gas​​exchange​​increases​​as​​:​
​-​ ​Surface​​area​​increases​
​-​ ​Diffusion​​distance​​decreases​
​-​ ​Diffusion​​gradient​​becomes​​more​​steep​

​Facilitated​​diffusion​​:​
​-​ ​Requires​​a​​channel​​protein​​in​​cell​​membrane​
​-​ ​Transports​​polar​​molecules,​​charged​​and​​water​​soluble​​molecules​​across​​the​​membrane​

​Osmosis​​:​
 ​-​ ​ iffusion​​of​​water​​from​​an​​area​​of​​low​​solute​​concentration​​to​​an​​area​​of​​high​​solute​​concentration​​through​​a​​partially​​permeable​
D
​membrane​
-​ ​ ​Diffusion​​of​​water​​from​​an​​area​​of​​high​​water​​potential​​to​​an​​area​​of​​low​​water​​potential​​through​​a​​partially​​permeable​​membrane​
​-​ ​Osmosis​​in​​animal​​cells​​:​
​-​ ​Hypotonic​​solution​​(higher​​water​​potential)​​:​
​-​ ​Water​​enters​​cell​​→​​Cytolysis​​(cell​​bursts)​
​-​ ​No​​cell​​wall​​→​​can​​withstand​​pressure​
​-​ ​Hypertonic​​solution​​(lower​​water​​potential)​​:​
​-​ ​Water​​leaves​​the​​cell​​→​​Cenation​​(cell​​shrivels)​
​-​ ​Fatal​​due​​to​​dehydration​
​-​ ​Isotonic​​:​
​-​ ​No​​net​​water​​movement​​→​​Cell​​stays​​the​​same​
​-​ ​Osmosis​​in​​plant​​cells​​:​
​-​ ​Hypotonic​​solution​​(higher​​water​​potential)​​:​
​-​ ​Water​​enters​​cell​​→​​Cell​​becomes​​turgid​
​-​ ​Turgid​​:​​plant​​rigidity​
​-​ ​Cell​​wall​​resists​​bursting​​→​​Supports​​plant​​structure​
​-​ ​Hypertonic​​solution​​(lower​​water​​potential)​​:​
​-​ ​Water​​leaves​​→​​Plasmolysis​
​-​ ​Protoplast​​pulls​​away​​from​​cell​​wall​
​-​ ​Cell​​shrinks​​but​​doesn’t​​collapse​​due​​to​​cell​​wall​
​-​ ​Isotonic​​solution​​:​
​-​ ​No​​net​​movement​​→​​Cell​​becomes​​flaccid​

​Active​​transport​​:​
​-​ ​Can​​transport​​all​​types​​of​​molecules​​through​​carrier​​proteins​
​-​ ​From​​an​​area​​of​​low​​concentration​​to​​an​​area​​of​​high​​concentration​
​-​ ​Active​​process​​←​​Requires​​energy​​in​​the​​form​​of​​ATP​

​Endocytosis​​:​
​-​ ​Transport​​large​​molecules​​and​​bulk​​transport​
​-​ ​Molecules​​are​​enclosed​​in​​vesicles​​made​​from​​the​​cell​​surface​​membrane​
​-​ ​Substances​​transported​​into​​the​​cell​
​-​ ​Phagocytosis​​:​
​-​ ​Uptake​​of​​solids​
​-​ ​Pinocytosis​
​-​ ​Uptake​​of​​liquids​

​Exocytosis​​:​
​-​ ​Transport​​large​​molecules​​and​​bulk​​transport​
​-​ ​Molecules​​are​​enclosed​​in​​vesicles​​made​​from​​the​​cell​​surface​​membrane​
​-​ ​Vesicles​​fuse​​with​​the​​cell​​surface​​membrane​​←​​Substances​​exit​​the​​cell​

​Cell​​division,​​Cell​​diversity​​and​​Cellular​​organisation​​:​

​Cell​​division​​and​​Cell​​Diversity​​:​

​The​​cell​​cycle​​:​
​-​ ​ he​​role​​of​​mitosis​​and​​the​​cell​​cycle​​is​​to​​produce​​identical​​daughter​​cells​​for​​growth​​and​
T
​asexual​​reproduction​​of​​cells​
-​ ​ ​During​​the​​cell​​cycle,​​a​​cell​​forms,​​it​​grows​​and​​then​​it​​divides​​to​​form​​daughter​​cells​
​-​ ​There​​are​​3​​main​​stages​​of​​the​​cell​​cycle​​and​​its​​controlled​​by​​checkpoints​​:​
​-​ ​Interphase​​:​
​-​ ​Cell​​grows,​​increases​​in​​mass​​and​​performs​​normal​​functions​​(E.g,​
​protein​​synthesis,​​DNA​​replication​
​-​ ​Prepares​​for​​mitosis​
​-​ ​G1​​+​​D​​+​​G2​
​-​ ​G1​​(Growth​​1)​​:​​Cells​​make​​RNA,​​enzymes​​and​​proteins​​for​
​growth.​​REvises​​signal​​to​​divide​​during​​this​​phase​
​-​ ​S​​(Synthesis)​​:​​DNA​​replication​​→​​each​​chromosome​​forms​
​2​​identical​​sister​​chromatids​
​-​ ​G2​​(Growth​​2)​​:​​Cell​​continues​​to​​grow,​​New​​DNA​​checked​
​for​​errors​​and​​repaired,​​Prepares​​for​​mitosis​​(E.g,​​makes​
​tubulin​​for​​spindle​​fibres)​
​-​ ​Nuclear​​division​​(Mitosis)​​:​
​-​ ​Cell​​growth​​stops​
​-​ ​Produces​​two​​genetically​​identical​​nuclei​
 ​-​ ​Cytokinesis​​:​
∴
​-​ ​Parent​​and​​replicated​​organelles​​move​​to​​opposite​​sides​​of​​the​​cell​​and​​the​​cytoplasm​​divides​​ ​​producing​​two​
​daughter​​cells​

​Cell​​cycle​​regulation​​:​
-​ ​ ​ nsures​​DNA​​is​​accurate​​before​​new​​cells​​are​​formed​
E
​-​ ​Errors​​during​​DNA​​replication​​(S​​phase)​​can​​cause​​mutations​
​-​ ​Proofreading​​and​​repair​​enzymes​​check​​and​​fix​​errors​
​-​ ​If​​damage​​is​​too​​severe,​​the​​cell​​may​​self-destruct​​(apoptosis)​​to​​prevent​​harm​

​Checkpoints​​:​
​1.​ ​G1​​Checkpoint​​:​
​-​ ​Checks​​for​​DNA​​damage​
​-​ ​If​​damaged,​​cell​​pauses​​before​​S​​phase​​for​​repairs​
​2.​ ​S​​Phase​​Checkpoint​​:​
​-​ ​Checks​​for​​DNA​​damage​
​-​ ​If​​damaged,​​the​​cell​​pauses​​before​​G2​​for​​repairs​
​3.​ ​G2​​Checkpoint​​:​
​-​ ​Checks​​for​​DNA​​damage​​after​​replication​
​-​ ​Repairs​​must​​be​​done​​before​​entering​​mitosis​
​4.​ ​Metaphase​​Checkpoint​​:​
​-​ ​ENsures​​chromosomes​​are​​properly​​attached​​to​​spindle​​fibres​​before​​anaphase​

​Mitosis​​:​
-​ ​ ​ ll​​cells​​produced​​by​​mitosis​​are​​genetically​​identical,​​therefore​​mitosis​​doesn’t​​give​​genetic​​variation​
A
​-​ ​P​rophase​​M​etaphase​​A​naphase​​T​elophase​​(PMAT)​
​Prophase​​:​
​-​ ​Nuclear​​envelope​​breaks​​down​​and​​disappeared​
​-​ ​Chromosomes​​condense​​and​​become​​visible​​with​​stains​
​-​ ​Centrioles​​move​​to​​opposite​​poles​​of​​the​​cell​​and​​start​​to​​form​​spindle​​fibres​

​Metaphase​​:​
​-​ ​Centrosomes​​are​​at​​opposite​​poles​​and​​spindle​​fibres​​are​​fully​​formed​
​-​ ​Chromosomes​​line​​up​​at​​the​​equator​​(metaphase​​plate)​
​-​ ​Spindle​​fibres​​attach​​to​​centromeres​​via​​kinetochores​
​-​ ​Each​​sister​​chromatid​​is​​connected​​to​ ​opposite​​poles​

​Anaphase​​:​
∴
​-​ ​Centromeres​​divide​​ ​​sister​​chromatids​​separate​
​-​ ​Spindle​​fibres​​shorten,​​pulling​​chromatids​​(now​​chromosomes​​to​​opposite​​poles)​

​Telophase​​:​
​-​ ​Chromosomes​​reach​​poles​​and​​decondense​
​-​ ​Nuclear​​envelopes​​reform​​around​​each​​set​
∴
​-​ ​Spindle​​fibres​​break​​down​​ ​​nucleoli​​reappear​

​Significance​​:​
​Growth​​:​
​-​ ​Enables​​a​​zygote​​to​​develop​​into​​a​​multicellular​​organism​
​-​ ​In​​plants,​​growth​​occurs​​in​​meristems​
​Cell​​Replacement​​and​​Tissue​​Repair​​:​
​-​ ​Replaces​​dead​​/​​damaged​​cells​​with​​identical​​ones​
​-​ ​Rapid​​replacement​​in​​skin​​and​​gut​​lining​
​-​ ​Some​​animals​​can​​regenerate​​parts​

​Asexual​​Reproduction​​:​
​-​ ​Offspring​​are​​clones​​of​​the​​parent​
​-​ ​In​​unicellular​​organisms,​​division​​=​​reproduction​
​-​ ​In​​multicellular​​organisms​​:​​budding​​(E.g,​​hydra,​​yeast),​​runners​​(E.g,​​strawberries)​

​Meiosis​​:​
-​ ​ ​ roduces​​4​​haploid​​(1​​set​​of​​chromosomes)​​cells​​from​​a​​diploid​​(2​​sets​​of​​chromosomes)​​cell​
P
​-​ ​Occurs​​in​​gamete​​(sex​​cell)​​formation​

​Meiosis​​1​​-​​Reduction​​Division​

​Prophase​​1​​:​
​-​ ​Chromosomes​​condense​​(Already​​replicated)​
​-​ ​Homologous​​chromosomes​​pair​​to​​form​​bivalents​
​-​ ​Crossing​​over​​between​​non-sister​​chromatids​​occurs​​at​​chiasmata​
​-​ ​Crossing​​over​​:​​Pairs​​of​​chromosomes​​line​​up​​and​​exchange​​some​​of​
​their​​genetic​​material​
​-​ ​Spindle​​forms​​;​​nuclear​​envelope​​and​​nucleolus​​break​​down​

​Metaphase​​1​​:​
​-​ ​Bivalents​​align​​at​​the​​equator​
​-​ ​Independent​​assortment​​of​​maternal​​and​​paternal​​chromosomes​
​-​ ​Independent​​assortment​​:​​There​​are​​various​​combinations​​of​
​chromosome​​arrangement​

​Anaphase​​1​​:​
​-​ ​Homologous​​chromosomes​​pulled​​to​​opposite​​poles​
​-​ ​Centromeres​​stay​​intact​

​Telophase​​1​​:​
​-​ ​Chromosomes​​reach​​poles​​;​​nuclear​​envelopes​​may​​reform​
​-​ ​Spindles​​break​​down​​(not​​always​​in​​plants)​

​Cytokinesis​​(After​​Meiosis​​1)​​:​
​-​ ​Cytoplasm​​divides​​→​​2​​haploid​​cells​
​-​ ​In​​animals​​:​​membrane​​pinches​​in​
​-​ ​In​​plants​​:​​Vesicles​​form​​cell​​plate​​and​​build​​cell​​wall​

​Meiosis​​2​​-​​Like​​Mitosis​​(No​​DNA​​replication​​before​​this)​

​Prophase​​II​​:​
​-​ ​Chromosomes​​condense​​again​​;​​spindle​​fibres​​reform​
 ​Metaphase​​II​​:​
​-​ ​Chromosomes​​line​​up​​single​​file​​on​​the​​equator​

​Anaphase​​II​​:​
​-​ ​Centromeres​​divide​​;​​chromatids​​pulled​​to​​opposite​​poles​

​Telophase​​II​​:​
​-​ ​Nuclear​​envelopes​​reform​​around​​4​​chromosome​​groups​

​Cytokinesis​​:​
​-​ ​Cytoplasm​​divides​​→​​4​​genetically​​unique​​haploid​​cells​

​Significance​​:​
-​ ​ C ​ reates​​genetic​​variation​​←​​Essential​​for​​natural​​selection​​and​​evolution​
​1.​ ​Crossing​​over​​(Prophase​​1)​​:​
​-​ ​Non-sister​​chromatids​​exchange​​alleles​​at​​points​​called​​chiasmata​
​-​ ​Leads​​to​​new​​allele​​combinations​​on​​chromosomes​
​-​ ​More​​likely​​to​​occur​​further​​from​​centromere​
​2.​ ​Independent​​assortment​​(Metaphase​​1)​​:​
​-​ ​Ransom​​alignment​​of​​homologous​​chromosome​​pairs​​at​​the​
​equator​
​-​ ​Each​​pair​​aligns​​independently​​→​​many​​possible​​chromosome​
​combinations​
​-​ ​Formula​​:​​2​n​ ​ ​(n​​=​​haploid​​number)​
​3.​ ​Random​​fusion​​of​​Gametes​​(Fertilisation)​​:​
​-​ ​Any​​sperm​​can​​fuse​​with​​any​​egg​
​-​ ​Combines​​two​​genetically​​unique​​gametes,​​creating​​a​​unique​​zygote​
​-​ ​Adds​​to​​genetic​​variation​​in​​offspring​

​Cellular​​Organisation​​:​
​ .​ T
1 ​ issues​​→​​Group​​of​​similar​​cells​​performing​​a​​specific​​function​
​2.​ ​Organs​​→​​Group​​of​​tissues​​working​​together​
​3.​ ​Organ​​systems​​→​​Groups​​of​​organs​​with​​related​​functions​

​Transport​​Cells​​in​​Plants​

​ ylem​​Vessel​​Cells​​:​
X ​ hloem​​Vessel​​Cells​​:​
P
​Function​​:​​Transport​​water​​&​​mineral​​ions​ ​Function​​:​​Transport​​sugars​​&​​amino​​acids​
​Adaptations​​:​ ​Adaptations​​:​
​-​ ​Dead,​​hollow​​cells​​form​​tubes​ ​-​ ​Living​​cells​​with​​sieve​​plates​​(perforated​​end​​walls)​
​-​ ​No​​top​​/​​bottom​​walls​​→​​continuous​​flow​ ​-​ ​Supported​​by​​companion​​cells​
​-​ ​Walls​​lignified​​→​​support​​&​​waterproof​ ​-​ ​Few​​organelles​​→​​easier​​flow​​of​​nutrients​

​Animal​​tissue​

​Muscle​​Cells​​:​ ​Ciliated​​Epithelium​​:​
 ​ unction​​:​​Contract​​to​​cause​​movement​
F ​ unction​​:​​Move​​substances​​(E.g​​mucus)​
F
​Adaptations​​:​ ​Adaptations​​:​
​-​ ​Contain​​protein​​filaments​​→​​contraction​ ​-​ ​Cilia​​beat​​in​​sync​​to​​shift​​mucus​
​-​ ​Many​​mitochondria​​→Energy​​for​​movement​ ​-​ ​Goblet​​cells​​secrete​​mucus​​to​​trap​​pathogens​
​-​ ​Skeletal​​muscle​​cells​​are​​multinucleated​

​ quamous​​Epithelium​​:​
S ​ artilage​​:​
C
​Function​​:​​Thin​​layer​​for​​diffusion​ ​Function​​:​​Support​​and​​flexibility​
​Adaptations​​:​ ​Adaptations​​:​
​-​ ​Single​​flat​​cell​​layer​​→​​short​ ​-​ ​Strong​​yet​​flexible​
​diffusion​​path​ ​connective​​tissue​
​-​ ​Permeable​​→​​Gas​ ​-​ ​Found​​in​​trachea​
​exchange​ ​(C-shaped​​rings)​​to​
​-​ ​Found​​in​​alveoli,​​blood​​vessels​ ​keep​​airway​​open​​and​
​flexible​

​Specialised​​Cells:​

​ rythrocytes​​(RBCs)​​:​
E
​Function​​:​​Transports​​O​​2​ ​and​​CO​​2​
​Adaptations​​:​
​-​ ​Biconcave​​shape​​-​​large​​surface​​area​
∴
​-​ ​No​​nucleus​​ ​​more​​space​​for​​haemoglobin​
∴
​-​ ​Flexible​​membrane​​ ​​can​​move​​through​​capillaries​
​-​ ​Lots​​of​​haemoglobin​​to​​bind​​O​2​ ​

​ eutrophils​​:​
N
​Function​​:​​Destroy​​pathogens​​by​​phagocytosis​
​Adaptations​​:​
∴
​-​ ​Flexible​​shape​​+​​nucleus​​ ​​can​​squeeze​​through​​capillaries​
​-​ ​Form​​pseudopodia​​to​​engulf​​microbes​
​-​ ​Many​​lysosomes​​-​​digest​​pathogens​

​ perm​​cells​​:​
S
​Function​​:​​Fertilise​​egg​​and​​pass​​on​​DNA​
​Adaptations​​:​
​-​ ​Acrosome​​-​​Enzymes​​to​​penetrate​​egg​
​-​ ​Haploid​​nucleus​​-​​½​​genetic​​material​
​-​ ​Many​​mitochondria​​-​​energy​​for​​movement​
​-​ ​Flagella​​(Tail)​​for​​movement​​/​​mobility​

​ oot​​Hair​​Cells​​:​
R
​Function​​:​​Absorb​​water​​+​​minerals​
​Adaptations​​:​
∴
​-​ ​Long​​extension​​ ​​Large​​surface​​area​
∴
​-​ ​Thin​​walls​​ ​​short​​diffusion​​path​
​-​ ​Vacuole​​with​​cell​​sap​​→​​water​​potential​​gradient​
​-​ ​Mitochondria​​→​​Active​​transport​
​-​ ​No​​chloroplasts​​(underground)​
 ​ iliated​​Epithelium​​:​
C
​Function​​:​​Move​​mucus​​+​​trapped​​particles​
​Adaptations​​:​
​-​ ​Cilia​​→​​coordinated​​movement​​to​​clear​​airways​
​-​ ​Goblet​​cells​​→​​secrete​​mucus​​to​​trap​​pathogens​

​ quamous​​Epithelium​​:​
S
​Function​​:​​Thin​​surface​​area​​for​​diffusion​​(E.g​​alveoli)​
​Adaptations​​:​
∴
​-​ ​One​​layer​​of​​flat​​cells​​ ​​short​​diffusion​​path​
​-​ ​Permeable​​→​​gas​​exchange​

​ alisade​​Cells​​:​
P
​Function​​:​​Photosynthesis​
​Adaptations​​:​
​-​ ​Many​​chloroplasts​​→​​max​​light​​absorption​
​-​ ​Tall,​​thin​​shape​​→​​dense​​packing,​​deep​​light​​penetration​

​ uard​​Cells​​:​
G
​Function​​:​​Regulate​​stomata​​for​​gas​​exchange​​+​​water​​loss​
​Adaptations​​:​
​-​ ​Uneven​​cell​​wall​​thickness​​→​​open​​/​​close​​stoma​
​-​ ​Many​​chloroplasts​​+​​mitochondria​​→​​energy​​for​​active​​processes​

​Stem​​cells​​:​
​-​ ​Can​​divide​​indefinitely​​by​​mitosis​

​After​​division,​​the​​new​​cells​​may​​:​
​-​ ​Remain​​stem​​cells​
​-​ ​Differentiate​​into​​a​​specialised​​cell​

​Porency​​:​​Ability​​to​​differentiate​

​Type​ ​Definition​ ​Examples​

​Totipotent​ ​Can​​become​​any​​cell,​​including​​embryo​​and​​placenta​​cells​ ​ ygote​​and​​cells​​up​​to​​16-​​cell​

Z
​stage​

​Pluripotent​ ​Can​​become​​any​​embryonic​​cell​​type​​(but​​not​​placenta​​cells)​ ​Embryonic​​stem​​cells​

​Multipotent​ ​Can​​become​​a​​limited​​range​​of​​cells​​related​​to​​their​​tissue​​of​​origin​ ​ dult​​stem​​cells,​​E.g,​​bone​​marrow​

A
​stem​​cells​

​Multiportent​​adult​​stem​​cells​​:​
-​ ​ ​ ound​​in​​developing​​tissues​​(E.g,​​bone​​marrow,​​brain,​​gut,​​heart,​​skin)​
F
​-​ ​Help​​with​​:​
​-​ ​Growth​
​-​ ​Cell​​replacement​
​-​ ​Tissue​​repair​
​-​ ​Can​​divide​​indefinitely​​but​​differentiate​​into​​limited​​cell​​types​
​Stem​​Cells​​in​​Animals​​and​​Plants​​:​

​Stem​​cells​​in​​bone​​marrow​​(Animals)​ ​ ype​​:​​Multipotent​​adult​​stem​​cells​
T
​Differentiate​​into​​:​
​-​ ​Erythrocytes​​(RBCs)​
​-​ ​Neutrophils​​(a​​type​​of​​white​​blood​​cell)​

​Erythrocytes​​(RBCs)​ ​ unction​​:​​Transport​​O​2​ ​ ​around​​body​

F
​Differentiation​​changes​​:​
​-​ ​Loss​​of​​nucleus​​(→​​no​​mitosis​​possible)​
​-​ ​Biconcave​​shape​​(Large​​surface​​area)​
​-​ ​Large​​Haemoglobin​​production​​(binds​​O​2​ ​​)​
​-​ ​Increased​​membrane​​flexibility​​(for​​capillary​​movement)​

​Neutrophils​​(White​​blood​​cells)​ ​ unction​​:​​Destroy​​pathogens​​by​​phagocytosis​
F
​Differentiation​​changes​​:​
​-​ ​Lobed​​nucleus​​(increased​​flexibility)​
​-​ ​Increased​​Lysosomes​
​-​ ​Increased​​membrane​​flexibility​​(helps​​movement​​through​​tissues)​

​Stem​​cells​​in​​Meristems​​(Plants)​ ​-​ ​Found​​in​​growing​​regions​​(E.g,​​root​​/​​shoot​​tips)​

​ ypes​​:​​Unspecialised​​plant​​stem​​cells​
T
​Key​​meristem​​:​​Cambium​
​-​ ​Located​​between​​xylem​​and​​phloem​

​Xylem​​cells​​(Water​​transport)​ ​Differentiation​​changes​​:​
​-​ ​Lignin​​deposited​​in​​walls​​(→Structural​​support)​
​-​ ​Loss​​of​​cytoplasm​
​-​ ​Loss​​of​​end​​walls​​(forms​​continuous​​tubes)​

​Phloem​​Sieve​​Tube​​Elements​ ​Differentiation​​changes​​:​
​-​ ​Reduced​​cytoplasm​​volume​
​-​ ​Loss​​of​​some​​organelles​
​-​ ​End​​walls​​become​​sieve​​plates​​(for​​assimilate​​flow)​

​Use​​of​​stem​​cells​​:​
​Stem​​cell​​therapy​​:​
​-​ ​Using​​adult​​stem​​cells​​to​​repair​​damaged​​tissue​​or​​treat​​disease​
​-​ ​Applications​​:​
​-​ ​Skin​​regeneration​​→​​for​​burn​​victims​
​-​ ​Neurons​​→​​for​​spinal​​cord​​injury​
​-​ ​Insulin-producing​​pancreas​​cells​​→​​for​​type​​1​​diabetes​
​-​ ​Retinal​​cells​​→​​for​​macular​​degeneration​
​Neurological​​Conditions​​:​
​-​ ​Alzheimer’s​​-​​Replace​​damaged​​brain​​cells​
​-​ ​Parkinson’s​​-​​Regenerate​​dopamine-producing​​neurons​
​Stem​​Cells​​in​​Developmental​​Biology​​:​
​-​ ​Embryonic​​stem​​cells​​can​​form​​all​​embryonic​​tissue,​​allowing​​scientists​​to​​:​
​-​ ​Study​​early​​human​​development​
​-​ ​Understand​​birth​​defects​
​-​ ​Investigate​​drug​​effects​​on​​embryos​
​Risks​​:​
​-​ ​Ethics​
​-​ ​Adult​​stem​​cells​​may​​cause​​rejection​​if​​not​​tissue-matched​
​-​ ​Stem​​cells​​can​​divide​​indefinitely​​;​​if​​uncontrolled,​​may​​form​​tumours​