Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 25, 2011, Pages 10150-10155

  Barua, Bipasha ^a   Pamula, Melissa C ^b   Hitchcock DeGregori, Sarah E ^a  

^a RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^b RUTGERS UNIVERSITY   (United States)

Author keywords

Actin filament structure; Cytoskeleton; Muscle regulation; Protein evolution

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ALANINE; ALPHA TROPOMYOSIN; F ACTIN; TROPOMYOSIN; TROPOMYOSIN COILED COIL; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ARTICLE; BINDING SITE; CIRCULAR DICHROISM; CNIDARIA; CODON; DIFFERENTIAL SCANNING CALORIMETRY; ESCHERICHIA COLI; MOLECULAR EVOLUTION; MUTAGENESIS; MUTATION; NONHUMAN; PHYLOGENETIC TREE; PRIORITY JOURNAL; SKELETAL MUSCLE; THERMOSTABILITY;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALORIMETRY, DIFFERENTIAL SCANNING; EVOLUTION, MOLECULAR; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHYLOGENY; PROTEIN BINDING; PROTEIN CONFORMATION; RATS; TROPOMYOSIN;

ANIMALIA; CHORDATA; CNIDARIA; ESCHERICHIA COLI; EUKARYOTA; RATTUS;

EID: 79959932890     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1101221108     Document Type: Article

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