N-terminal strands of filamin Ig domains act as a conformational switch under biological forces

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 1, 2010, Pages 12-24

  Kesner, Barry A ^a   Ding, Feng ^a   Temple, Brenda R ^a   Dokholyan, Nikolay V ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

Discrete molecular dynamics (DMD); Filamin; Forced unfolding; Ig domain; Thermal unfolding

Indexed keywords

FILAMIN A; ACTIN BINDING PROTEIN; CONTRACTILE PROTEIN; FILAMINS;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CELL STRESS; CONFORMATIONAL TRANSITION; DIMERIZATION; IMMUNOGLOBULIN LIKE DOMAIN; MECHANICAL STRESS; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DOMAIN; SOLVATION; TEMPERATURE DEPENDENCE; THERMOSTABILITY; CHEMISTRY; HUMAN; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

CONTRACTILE PROTEINS; HUMANS; MICROFILAMENT PROTEINS; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE;

EID: 77949381923     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22479     Document Type: Article

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