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 journalArticlepeer-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 languageEnglish
Pages (from-to)543-547
Number of pages5
JournalJournal of Molecular Biology
Volume413
Issue number3
DOIs
StatePublished - Oct 28 2011

Keywords

  • NMR
  • X-ray crystallography
  • hydrogen bond
  • protein folding
  • villin headpiece

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