TY - JOUR
T1 - On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece
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 - http://www.scopus.com/inward/record.url?scp=80054682536&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2011.08.024
DO - 10.1016/j.jmb.2011.08.024
M3 - Article
C2 - 21903098
AN - SCOPUS:80054682536
VL - 413
SP - 543
EP - 547
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 3
ER -