Literature DB >> 9164455

NMR structure of the 35-residue villin headpiece subdomain.

C J McKnight, P T Matsudaira, P S Kim.   

Abstract

The NMR structure of an autonomously folding subdomain from villin headpiece is reported. It forms a novel three helix structure with the actin-binding residues arrayed on the C-terminal helix.

Mesh：

Substances：

Year:  1997        PMID： 9164455     DOI： 10.1038/nsb0397-180

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN： 1072-8368


  86 in total

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3.  The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain.

Authors:  Benjamin S Frank; Didem Vardar; Deirdre A Buckley; C James McKnight
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4.  Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements.

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6.  Simple few-state models reveal hidden complexity in protein folding.

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7.  Hydrophobic core formation and dehydration in protein folding studied by generalized-ensemble simulations.

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8.  The unusual internal motion of the villin headpiece subdomain.

Authors:  Kyle W Harpole; Evan S O'Brien; Matthew A Clark; C James McKnight; Liliya Vugmeyster; A Joshua Wand
Journal:  Protein Sci       Date:  2015-10-29       Impact factor: 6.725

9.  Characterizing a partially ordered miniprotein through folding molecular dynamics simulations: Comparison with the experimental data.

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Journal:  Protein Sci       Date:  2015-12-16       Impact factor: 6.725

10.  Detection of a transient intermediate in a rapid protein folding process by solid-state nuclear magnetic resonance.

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Journal:  J Am Chem Soc       Date:  2010-01-13       Impact factor: 15.419
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