The helix located between the two domains of a Mip-like peptidyl-prolyl cis - Trans isomerase is crucial for its structure, stability, and protein folding ability

Biochemistry

Volumn 51, Issue 40, 2012, Pages 7930-7939

  Jana, Biswanath ^a   Sau, Subrata ^a  

^a BOSE INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; CIS-TRANS; DELETION MUTANTS; E. COLI; IMMUNOSUPPRESSIVE DRUGS; IN-VITRO; INSERTION MUTANTS; ISOMERASES; MOLECULAR DIMENSIONS; MUTANT PROTEINS; RAPAMYCIN; RECOMBINANT E. COLI; SECONDARY STRUCTURES; TERTIARY STRUCTURES; TWO DOMAINS; TWO-STATE; VIRULENCE FACTORS;

BINDING ENERGY; ESCHERICHIA COLI; PROTEIN FOLDING; UREA;

RECOMBINANT PROTEINS;

ISOMERASE; MIP LIKE PEPTIDYLPROLYL ISOMERASE; PROTEIN FKBP22; RAPAMYCIN; UNCLASSIFIED DRUG; UREA;

ALPHA HELIX; ARTICLE; BINDING AFFINITY; DIMERIZATION; DRUG PROTEIN BINDING; GENE DELETION; GENE INSERTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; MODELS, MOLECULAR; MOLECULAR SEQUENCE ANNOTATION; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; RECOMBINANT PROTEINS; TACROLIMUS BINDING PROTEINS; UREA;

EID: 84867449333     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300720g     Document Type: Article

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