PROTEIN
A. Amino Acids
Amino acids are molecules used by all living things to
make proteins. Your body needs 20 different amino
acids to function correctly. Nine of these amino acids
are called essential amino acids. Essential amino acids
must be consumed through the food you eat. Essential
amino acids can be found in a variety of foods,
including beef, eggs, and dairy
B. Special amino acide: Cystein
Cysteine is considered a semi-essential amino
acid that is crucial for protein building and the
formation of disulfide bonds, which are vital for
protein structure and stability.
C. Peptides and Protein
Peptides and protein are both biological molecules made of
amino acids linked by peptides bonds. The key difference lies
in their size; peptides are shorter chains (typically 2-50 amino
acids), while protein are larger, longer chains (often over 50
amino acids). Both play crucial roles in cellular function, with
proteins acting as structural and functional components and
peptides often functioning as signaling molecules.
D. Structure of Protein
Proteins are complex molecules with four levels of
structure: primary, secondary, tertiary, and
quaternary. The primary structure is the linear sequence
of amino acids.
E. Primary Structure of Protein
This is the linear sequence of amino acids linked by
peptide bonds. It dictates the proteins overall shape and
function. Proteins are synthesized from the N-terminus to
the C-terminus.
F. Secondary structure of Protein
Local folding patterns within the polypeptide chains,
stabilized by hydrogen bonds. Common examples
include the alpha-helix and beta- pleated sheet.
Alpha- helices are coiled structures, while beta-
pleated sheets are formed by parallel or anti- parallel
polypeptide stands.
G. Tertiary Structure of Protein
The three dimensional structure of a single
polypeptide chain, resulting from interactions
between amino acid side chains (R-groups). These
interactions include hydrogen bonds, ionic bonds,
hydrophobic interactions and disulfide bonds. These
tertiary structure determines the proteins overall
shape and functional activity.
Quaternary Structure
The arrangement of multiple polypeptide
chains(subunits)to form a functional protein. Not all
protein have a quaternary structure; it depends on
the proteins function and complexity. Subunits can be
identical or different, and their interactions are crucial
for the proteins activity.
Glycoprotein
A glycoprotein is a protein with one or more
covalently attached carbohydrate chains, a
process called glycosylation. These sugar
chains, or glycans, can be attached to
specific amino acids like asparagine (N-
linked) or serine/threonine (O-linked).
Glycoproteins perform diverse functions,
including structural support (collagen),
immune responses (immunoglobulins),
transport (transferrin), cell recognition,
lubrication (mucins), and even acting as