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Protein Structure: Types and Examples

The document discusses different levels of protein structure including primary, secondary, tertiary, and quaternary structure. It provides details on common secondary structures like alpha helices and beta sheets. Alpha helices are stabilized by hydrogen bonds between residues that are 4 positions apart in the amino acid sequence in a right-handed coil. Beta sheets can be either parallel or anti-parallel and are stabilized by inter-strand hydrogen bonds. Examples of fibrous proteins that are dominated by a single secondary structure like collagen and keratin are provided. Collagen contains a repeating motif of three peptide chains that form a right-handed supercoil stabilized by hydrogen bonds. Alpha keratin contains two intertwined alpha helices that form a left-handed

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Amos Josephat
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10 views21 pages

Protein Structure: Types and Examples

The document discusses different levels of protein structure including primary, secondary, tertiary, and quaternary structure. It provides details on common secondary structures like alpha helices and beta sheets. Alpha helices are stabilized by hydrogen bonds between residues that are 4 positions apart in the amino acid sequence in a right-handed coil. Beta sheets can be either parallel or anti-parallel and are stabilized by inter-strand hydrogen bonds. Examples of fibrous proteins that are dominated by a single secondary structure like collagen and keratin are provided. Collagen contains a repeating motif of three peptide chains that form a right-handed supercoil stabilized by hydrogen bonds. Alpha keratin contains two intertwined alpha helices that form a left-handed

Uploaded by

Amos Josephat
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© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd

Previous lecture: Protein Structure

Primary

a.a. sequence
peptide bond
Planar : to describe rotation about the C(O)-N bond and involves
the C()-C(O)-N-C() bonds
Two rotatable torsions; : rotation about the N-C() bond; :
rotation about the C()-C(O)

Ramachandran plot

Levels of Protein Structure


Primary:
a.a. sequence
Secondary:
repeat structural motifs
Tertiary: overall 3D conformation

Quarternary: organization (spatial) of


multiple subunits

Secondary Structures
a-helix
b-sheet
turn

loop

a-helix: a coiled structure stabilized by


intra-chain H-bond within the backbone

a-helix
H-bond between carboxyl of ith residue and the
amide of the i+4 residue.

3.6 residue/turn
Translation = 1.5 per residue
Pitch = 5.4 (1.5 3.6)
Almost exclusively Right handed.
See for yourself
[Link]

b-sheets are stabilized by inter-strand H-bonds

Backbone fully extended


Adjacent side-chains point in opposite direction
Periodicity of 2

Anti-parallel b-sheet

Parallel b-sheet

See for yourself


[Link]

A reverse turn

Tertiary Structure (Protein)


Fibrous proteins
Contains stiff, elongated, fibrous regions; tend to be
insoluble and strong
Serves a protective, connective, or supportive role
Dominated by a single type of 2nd structure
Globular proteins
Complex shapes with more than one type of 2nd
structure
Serve as Enzymes; Hormones; Antibodies;
Some structural proteins: Globular proteins form part of
the cell membrane, which has a structural role as well as
a role in transporting ions in and out of the cell

Fibrous Proteins:
Keratins: found in hair, fingernails, and bird feathers

Collagens the most abundant proteins in a


vertebrate body, found in connective tissues such as
cartilage
Elastins, found in ligaments, around blood vessels.

Collagen
The basic structural unit is
tropocollagen , which consists of
three intertwined peptide chains of
~1000 amino acids each.

The intertwining is such that stable


hydrogen bonds are formed
between the strands to form a righthanded super-helical cable

There is a frequent G-P-X or GX-hydroxyP motif, where X can be


any amino acid.

H-bond within each single


peptide stand is absent; Steric
repulsion between P or hydroyP
stabilize a left-handed helix

Check out: [Link]; [Link]

Every third residue faces towards the


inside of the helix. Sterically, only glycine
will fit.

a-keratin
Two right-handed a-helix intertwinded to form a left-handed
super-helix called a coiled coil.

Two a-helices held together by van der Waals or chargecharge interactions


Some keratins have disulfide bonds between Cys residues in
different chains.

Nat Struct Mol Biol, 19, 707-715. (2012) doi:


10.1038/nsmb.2330

[Link]

Implications for epidermolysis bullosa simplex

Occurrence of a homotypic disulfide bond via K14 Cys367

Linking the disulfide bond to function

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