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.
authors: Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA.
authors: Jeffrey W
authors: JW
authors: Brown
authors: Jeremiah D
authors: JD
authors: Farelli
authors: C James
authors: CJ
authors: McKnight
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D018360:Crystallography, X-Ray; D004330:Drosophila / Q000378:metabolism; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017354:Point Mutation / Q000235:genetics; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary
chemical_list: D000199:Actins; D008840:Microfilament Proteins; C026615:villin