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Fibrous Proteins Examples 1. a-keratins 2. Silk Fibroin 3. Collagen

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Presentation on theme: "Fibrous Proteins Examples 1. a-keratins 2. Silk Fibroin 3. Collagen"— Presentation transcript:

1 Fibrous Proteins Examples 1. a-keratins 2. Silk Fibroin 3. Collagen
Hair, nails, horns, skin 2. Silk Fibroin 3. Collagen 4. Elastin Saw Varsity’s a-keratins off

2 Amino Acid Composition of Fibrous Proteins
-Keratin (Wool) Fibroin (Silk) Collagen (Tendon) Elastin (Aorta) Gly Ala Ser Glu + Gln Cys tr. Pro Arg Leu Thr Asp + Asn Val Tyr Ile Phe His tr. Met tr. Trp tr.

3 -Keratin

4 Keratin: an Intermediate Filament Protein
What’s in Hair and Wool?

5 Collagen Intramolecular Crosslinks Intermolecular Crosslinks
b a’ Gly-X-Y a Left hand -helix X=Pro Y=HO-Pro Intermolecular Crosslinks Quarter Stagger

6 ELASTIN Property of Resilience 4-way Stretch Aorta Lung
Ligamentum Nuchae

7 Tertiary Structure Overall Shape (applies mainly to globular proteins)
Alpha helix Beta structure Structural Motifs Beta barrel Beta-alpha-beta

8 Globular Protein Molecules
3-Dominant Structural Features Helix a Beta Sheet Turns or loops Typical Protein Packs Framework Connects

9 Rules Governing Protein Folding
Can we predict how a protein will fold on the basis of amino acid sequence data alone? 1. Globular Proteins have a defined outside and inside Hydrophobic buried inside Hydrophilic outside

10 Folding and Biological Activity
Enzyme Active Site Z X Y X Z Y Random Coil Folded Denatured Biologically Active

11 TURNS (on Surfaces) Reverse direction abruptly
Beta Bends or Turns (4 residues to execute sharp turn) H-bonding between carbonyl residue1 and amide N on residue 3. Glycine not in loop (Type I turn) Glycine in loop (Type II turn) Gamma (very tight turn) Proline in loop, bonding between 1 and 2 Tight Turn

12 Reverse Turn in Polypeptides
Glycine H-bond between 1 and 4 Twice more common than type 2

13 Chou-Fasman Rule for Predicting Secondary Structure
Propensity Helix Beta Sheet Beta Turn

14 Protein Folding Mystery
To fold a protein is negative entropy with respect to the protein. You go from a disordered to an ordered state. Folding is away from a natural tendency to exist in a random state? Where is the energy driving protein folding? ANSWER IN TEXTBOOK

15 ANSWER DSTotal = DSsys - DSsurround ORGANIZED WATER N C Folded N C
Unfolded ORGANIZED WATER DSTotal = DSsys - DSsurround

16 QUATERNARY STRUCTURE SUBUNIT STRUCTURE Multisubunit Proteins HOMODIMER
HETERODIMER

17 WEAK FORCES IN PROTEIN

18 Hydropathic Index + hydrophobic _ hydrophilic

19 Determining Hydropathic Index
Sum 1-9 (window) Sum 2-10 Sum 3-11 Sum 4-12 Sum 5-13 Sum 6-14 (-) (+)

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