The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function

Journal of Biological Chemistry

Volumn 286, Issue 5, 2011, Pages 3863-3872

  Morrone, Angela ^a   McCully, Michelle E ^b   Bryan, Philip N ^c   Brunori, Maurizio ^a   Daggett, Valerie ^b   Gianni, Stefano ^a   Travaglini Allocatelli, Carlo ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b University of Washington   (United States)

^c UNIVERSITY OF MARYLAND   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTATIONAL TECHNIQUE; DENATURED STATE; DIFFERENT STRUCTURE; FOLDING MECHANISM; FOLDING PATHWAY; HELICAL STRUCTURES; NATIVE STATE; NATIVE STRUCTURES; PROTEIN FOLDING PROBLEM; PROTEIN TOPOLOGY; RESIDUAL STRUCTURE; SEQUENCE IDENTITY;

AMINO ACIDS; PROTEIN FOLDING; TOPOLOGY;

DENATURATION;

PROTEIN G; PROTEIN G A88; PROTEIN G B88; UNCLASSIFIED DRUG; PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; BIOPHYSICS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; MOLECULAR DYNAMICS; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTEIN VARIANT; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; CHEMISTRY; PROTEIN CONFORMATION; PROTEIN ENGINEERING;

AMINO ACID SEQUENCE; HYDROGEN-ION CONCENTRATION; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEINS;

EID: 79952805688     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.155911     Document Type: Article

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