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17_April_Sample_Proteins

17_April_Sample_Proteins

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Published by: Ruth Danielle Gascon on Apr 05, 2011
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1
Alpha Keratin
Found in hair, fingernails, claws, horns andbeaksSequence consists of 311-314 residuealpha helical rod segments capped withnon-helical N- and C-terminiPrimary structure of helical rods consistsof 7-residue repeats: (a-b-c-d-e-f-g)
n
,where a and d are nonpolar. Promotesassociation of helices!
(a)
Both type I and type II
α 
-keratin molecules have sequences consisting of long,central rod domains with terminal cap domains. The numbers of amino acid residues ineach domain are indicated. Asterisks denote domains of variable length.
(b)
The roddomains form coiled coils consisting of intertwined right-handed
α 
-helices. These coiledcoils then wind around each other in a left-handed twist. Keratin filaments consist oftwisted protofibrils (each a bundle of four coiled coils).
(
Adapted from Steinert, P., and Parry,D., 1985 
. Annual Review of Cell Biology
1:
41–65 
;
and Cohlberg, J., 1993.
Trends in BiochemicalSciences
18:
360–362 
.)
 
2
Beta Keratin
Proteins that form extensive beta sheets 
Found in silk fibersAlternating sequence:Gly-Ala/Ser-Gly-Ala/Ser....Since residues of a beta sheet extendalternately above and below the plane of thesheet, this places all glycines on one side andall alanines and serines on other side!This allows Glys on one sheet to mesh withGlys on an adjacent sheet (same for Ala/Sers)
Silk fibroin consists of a unique stacked array of
β 
-sheets. The primary structure offibroin molecules consists of long stretches of alternating glycine and alanine or serineresidues. When the sheets stack, the more bulky alanine and serine residues on oneside of a sheet interdigitate with similar residues on an adjoining sheet. Glycinehydrogens on the alternating faces interdigitate in a similar manner, but with a smallerintersheet spacing.
(Illustration: Irving Geis. Rights owned by Howard Hughes Medical Institute. Not to be reproduced without permission.)
 
3
Collagen - A Triple Helix
Principal component of connective tissue (tendons, cartilage, bones, teeth)
basic unit is tropocollagen:three intertwined polypeptide chains(1000 residues each)MW = 285,000300 nm long, 1.4 nm diameterunique amino acid composition
Collagen
The secrets of its a.a. composition...
Nearly one residue out of three is GlyProline content is unusually highUnusual amino acids found:4-hydroxyproline3-hydroxyproline5-hydroxylysinePro and HyPro together make 30% ofres.

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