Literature DB >> 19431311

Studies on the Structure of Feather Keratin: II. A beta-Helix Model for the Structure of Feather Keratin.

R Schor, S Krimm.   

Abstract

The assumption that the proline residues in feather keratin, which comprise 12 per cent of the total, are periodically located along the polypeptide chain is shown to lead to an essentially unique structure for this fibrous protein. The structure is based on a beta-helix; i.e., an extended chain which coils slowly to form a helix of relatively large pitch. Such helices tend to aggregate by hydrogen bonding to form cylindrical units, which in turn can aggregate further into cable-like structures. This model has been tested with respect to its predictions concerning the x-ray diffraction pattern, infrared spectrum, mechanical properties, and chemical behavior of feather keratin. Preliminary results indicate that it is better capable of accounting for the data than previously proposed structures.

Entities:  

Year:  1961        PMID: 19431311      PMCID: PMC1366335          DOI: 10.1016/s0006-3495(61)86904-x

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  12 in total

1.  Models of alpha-keratin sturcture.

Authors:  R D FRASER; T P MACRAE; D H SIMMONDS
Journal:  Biochim Biophys Acta       Date:  1957-09

2.  Role of proline in polypeptide chain configuration of proteins.

Authors:  A G SZENT-GYORGYI; C COHEN
Journal:  Science       Date:  1957-10-11       Impact factor: 47.728

3.  Protein structure in relation to function and biosynthesis.

Authors:  C B ANFINSEN; R R REDFIELD
Journal:  Adv Protein Chem       Date:  1956

4.  Cylindrical lattice structure of collagen.

Authors:  G N RAMACHANDRAN; V SASISEKHARAN
Journal:  Arch Biochem Biophys       Date:  1956-07       Impact factor: 4.013

5.  Structure and composition of soluble feather keratin.

Authors:  A M WOODIN
Journal:  Biochem J       Date:  1956-08       Impact factor: 3.857

6.  Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type.

Authors:  L PAULING; R B COREY
Journal:  Nature       Date:  1953-01-10       Impact factor: 49.962

7.  Hydrogen Bonded Helical Configurations of the Polypeptide Chain.

Authors:  J Donohue
Journal:  Proc Natl Acad Sci U S A       Date:  1953-06       Impact factor: 11.205

8.  Two Rippled-Sheet Configurations of Polypeptide Chains, and a Note about the Pleated Sheets.

Authors:  L Pauling; R B Corey
Journal:  Proc Natl Acad Sci U S A       Date:  1953-04       Impact factor: 11.205

9.  Studies on the Structure of Feather Keratin: I. X-Ray Diffraction Studies and Other Experimental Data.

Authors:  R Schor; S Krimm
Journal:  Biophys J       Date:  1961-07       Impact factor: 4.033

10.  The pleated sheet, a new layer configuration of polypeptide chains.

Authors:  L PAULING; R B COREY
Journal:  Proc Natl Acad Sci U S A       Date:  1951-05       Impact factor: 11.205

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  4 in total

Review 1.  The role of β-sheets in the structure and assembly of keratins.

Authors:  R D Bruce Fraser; David A D Parry
Journal:  Biophys Rev       Date:  2009-01-23

2.  Soluble derivatives of feather keratin. 2. Molecular weight and conformation.

Authors:  B S Harrap; E F Woods
Journal:  Biochem J       Date:  1964-07       Impact factor: 3.857

3.  Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba.

Authors:  S Pabisch; S Puchegger; H O K Kirchner; I M Weiss; H Peterlik
Journal:  J Struct Biol       Date:  2010-07-15       Impact factor: 2.867

4.  Development of feather keratin during embryogenesis of the chick.

Authors:  E BELL; Y T THATHACHARI
Journal:  J Cell Biol       Date:  1963-02       Impact factor: 10.539

  4 in total

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