How to Arm a Supervillin: Designing F-Actin Binding Activity into Supervillin Headpiece

Journal of Molecular Biology

Volumn 393, Issue 3, 2009, Pages 608-618

  Brown, Jeffrey W ^a   Vardar Ulu, Didem ^b   McKnight, C James ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b WELLESLEY COLLEGE   (United States)

Author keywords

electrostatic surface potential; NMR structure and relaxation; protein design; supervillin; villin type headpiece domain

Indexed keywords

ACTIN BINDING PROTEIN; ERYTHROCYTE BAND 4.9 PROTEIN; LEUCINE; LYSINE; NITROGEN 15; VILLIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; HUMAN; MUTAGENESIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; REGULATORY MECHANISM;

EID: 70349785050     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.018     Document Type: Article

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