The flexibility of two tropomyosin mutants, D175N and E180G, that cause hypertrophic cardiomyopathy

Biochemical and Biophysical Research Communications

Volumn 424, Issue 3, 2012, Pages 493-496

  Li, Xiaochuan Edward ^a   Suphamungmee, Worawit ^a   Janco, Miro ^b   Geeves, Michael A ^b   Marston, Steven B ^c   Fischer, Stefan ^d   Lehman, William ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF KENT   (United Kingdom)

^c NATIONAL HEART AND LUNG INSTITUTE   (United Kingdom)

^d UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

Actin; Cardiomyopathy; Electron microscopy; Molecular Dynamics; Tropomyosin

Indexed keywords

ASPARTIC ACID; CALCIUM ION; F ACTIN; GLUTAMIC ACID; MYOSIN; TROPOMYOSIN;

ARTICLE; BINDING SITE; DIASTOLIC DYSFUNCTION; ELECTRON MICROSCOPY; HEART FAILURE; HEART MUSCLE; HYPERTROPHIC CARDIOMYOPATHY; MOLECULAR DYNAMICS; MUTANT; PRIORITY JOURNAL; PROTEIN BINDING; SIMULATION; STRUCTURE ANALYSIS; SYSTOLE;

ACTINS; AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTIC ACID; CALCIUM; CARDIOMYOPATHY, HYPERTROPHIC; GLUTAMIC ACID; GLYCINE; HUMANS; MICROSCOPY, ELECTRON; MODELS, CHEMICAL; MOLECULAR DYNAMICS SIMULATION; MUTATION; MYOSINS; PROTEIN STRUCTURE, SECONDARY; TROPOMYOSIN;

EID: 84864767294     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.06.141     Document Type: Article

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