On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece

Jeffrey W. Brown; Jeremiah D. Farelli; C. James McKnight

doi:10.1016/j.jmb.2011.08.024

On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece

Jeffrey W. Brown
, Jeremiah D. Farelli
, C. James McKnight

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Villin headpiece is a small autonomously folding protein that has emerged as a model system for understanding the fundamental tenets governing protein folding. In this communication, we employ NMR and X-ray crystallography to characterize a point mutant, H41F, which retains actin-binding activity, is more thermostable but, interestingly, does not exhibit the partially folded intermediate observed of either wild-type or other similar point mutants.

Original language	English
Pages (from-to)	543-547
Number of pages	5
Journal	Journal of Molecular Biology
Volume	413
Issue number	3
DOIs	https://doi.org/10.1016/j.jmb.2011.08.024
State	Published - Oct 28 2011

Keywords

NMR
X-ray crystallography
hydrogen bond
protein folding
villin headpiece

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10.1016/j.jmb.2011.08.024

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title = "On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece",

abstract = "Villin headpiece is a small autonomously folding protein that has emerged as a model system for understanding the fundamental tenets governing protein folding. In this communication, we employ NMR and X-ray crystallography to characterize a point mutant, H41F, which retains actin-binding activity, is more thermostable but, interestingly, does not exhibit the partially folded intermediate observed of either wild-type or other similar point mutants.",

keywords = "NMR, X-ray crystallography, hydrogen bond, protein folding, villin headpiece",

author = "Brown, \{Jeffrey W.\} and Farelli, \{Jeremiah D.\} and McKnight, \{C. James\}",

note = "Funding Information: We thank Liliya Vugmeyster for her guidance with relaxation dispersion experiments. Financial support was provided by a Boston University Graduate Student Research Fellowship to J.W.B. and the National Institutes of Health Grant GM62886 to C.J.M. ",

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AU - Brown, Jeffrey W.

AU - Farelli, Jeremiah D.

AU - McKnight, C. James

N1 - Funding Information: We thank Liliya Vugmeyster for her guidance with relaxation dispersion experiments. Financial support was provided by a Boston University Graduate Student Research Fellowship to J.W.B. and the National Institutes of Health Grant GM62886 to C.J.M.

PY - 2011/10/28

Y1 - 2011/10/28

N2 - Villin headpiece is a small autonomously folding protein that has emerged as a model system for understanding the fundamental tenets governing protein folding. In this communication, we employ NMR and X-ray crystallography to characterize a point mutant, H41F, which retains actin-binding activity, is more thermostable but, interestingly, does not exhibit the partially folded intermediate observed of either wild-type or other similar point mutants.

AB - Villin headpiece is a small autonomously folding protein that has emerged as a model system for understanding the fundamental tenets governing protein folding. In this communication, we employ NMR and X-ray crystallography to characterize a point mutant, H41F, which retains actin-binding activity, is more thermostable but, interestingly, does not exhibit the partially folded intermediate observed of either wild-type or other similar point mutants.

KW - NMR

KW - X-ray crystallography

KW - hydrogen bond

KW - protein folding

KW - villin headpiece

UR - https://www.scopus.com/pages/publications/80054682536

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DO - 10.1016/j.jmb.2011.08.024

M3 - Article

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SP - 543

EP - 547

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 3

ER -

On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece

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Keywords

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