Literature DB >> 7632873

Alpha-helix formation by peptides of defined sequence.

R L Baldwin1.   

Abstract

The factors controlling alpha-helix formation in water by peptides of defined sequence are beginning to be understood. The field is close to the point where the extent of helix formation can be predicted for peptides of any sequence. Our own approach to the problem, and the main results obtained by following this approach, are summarized below. The chief reason for studying alpha-helix formation by peptides is to understand precisely and in detail one part of the protein folding problem. Questions about peptide helix formation can be answered at a fundamental level, in terms of the physico-chemical mechanisms involved.

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Year:  1995        PMID: 7632873     DOI: 10.1016/0301-4622(94)00146-b

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  28 in total

1.  The effects of alpha-helix on the stability of Asn residues: deamidation rates in peptides of varying helicity.

Authors:  A A Kosky; U O Razzaq; M J Treuheit; D N Brems
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

2.  The turn sequence directs beta-strand alignment in designed beta-hairpins.

Authors:  E de Alba; M Rico; M A Jiménez
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

3.  Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.

Authors:  S Padmanabhan; M A Jiménez; M Rico
Journal:  Protein Sci       Date:  1999-08       Impact factor: 6.725

4.  Comparative conformational analysis of peptide libraries.

Authors:  S G Jacchieri
Journal:  Mol Divers       Date:  1998       Impact factor: 2.943

5.  WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state.

Authors:  E K Koepf; H M Petrassi; M Sudol; J W Kelly
Journal:  Protein Sci       Date:  1999-04       Impact factor: 6.725

6.  Influence of the C-terminus of the glycophorin A transmembrane fragment on the dimerization process.

Authors:  M Orzáez; E Pérez-Payá; I Mingarro
Journal:  Protein Sci       Date:  2000-06       Impact factor: 6.725

7.  Parallel β-sheet secondary structure is stabilized and terminated by interstrand disulfide cross-linking.

Authors:  Aaron M Almeida; Rebecca Li; Samuel H Gellman
Journal:  J Am Chem Soc       Date:  2011-12-13       Impact factor: 15.419

8.  Solution structure and dynamics of a de novo designed three-helix bundle protein.

Authors:  S T Walsh; H Cheng; J W Bryson; H Roder; W F DeGrado
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-11       Impact factor: 11.205

9.  Exploring atomistic details of pH-dependent peptide folding.

Authors:  Jana Khandogin; Jianhan Chen; Charles L Brooks
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-20       Impact factor: 11.205

10.  Electron-electron distances in spin-labeled low-spin metmyoglobin variants by relaxation enhancement.

Authors:  Dmitriy Ulyanov; Bruce E Bowler; Gareth R Eaton; Sandra S Eaton
Journal:  Biophys J       Date:  2008-09-05       Impact factor: 4.033

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