Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation

Journal of Biological Chemistry

Volumn 286, Issue 3, 2011, Pages 2041-2046

  Cheng, Haiming ^a   Rashid, Shayan ^a   Yu, Zhuoxin ^a   Yoshizumi, Ayumi ^a   Hwang, Eileen ^a   Brodsky, Barbara ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

C TERMINUS; COLLAGEN PROTEINS; HELIX NUCLEATION; MOLECULAR POPULATION; N-TERMINALS; OSTEOGENESIS IMPERFECTA; SEQUENCE PATTERNS; SIGNIFICANT IMPACTS; SITE DIRECTED MUTAGENESIS; TRIMERIZATION; TYPE I COLLAGEN;

AMINO ACIDS; BACTERIOLOGY; CHEMICAL REACTIONS; CONFORMATIONS;

COLLAGEN;

BACTERIAL PROTEIN; COLLAGEN TYPE 1; GLYCINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SITE DIRECTED MUTAGENESIS; STREPTOCOCCUS PYOGENES; TRIPLE HELIX;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; COLLAGEN; GLYCINE; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; STREPTOCOCCUS PYOGENES;

BACTERIA (MICROORGANISMS);

EID: 78751521383     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.153965     Document Type: Article

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