Conformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7-Reference-Cited by-同舟云学术

Conformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7

Published:2013-10-19 Issue:12 Volume:22 Page:1722-1738
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Figueiredo Angelo Miguel¹,Whittaker Sara B.-M.²,Knowling Stuart E.³,Radford Sheena E.³,Moore Geoffrey R.¹

Affiliation:

1. Centre for Structural and Molecular Biochemistry, School of Chemistry; University of East Anglia; Norwich NR4 7TJ United Kingdom

2. The Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences; University of Birmingham; Vincent Drive Birmingham B15 2TT United Kingdom

3. Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology; University of Leeds; Leeds LS2 9JT United Kingdom

Funder

Wellcome Trust, Wolfson Foundation, and Biotechnology and Biological Sciences Research Council

Fundação para a Ciência e Tecnologia, Portugal

Engineering and Physical Sciences Research Council

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2372/fullpdf

Reference82 articles.

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3. Application of the diffusion-collision model to the folding of three-helix bundle proteins;Islam;J Mol Biol,2002

4. Fast folding of a helical protein initiated by the collision of unstructured chains;Meisner;Proc Natl Acad Sci USA,2004

5. Prediction of protein folding rates from the amino acid sequence-predicted secondary structure;Ivankov;Proc Natl Acad Sci USA,2004

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