The native GCN4 leucine-zipper domain does not uniquely specify a dimeric oligomerization state

Biochemistry

Volumn 51, Issue 47, 2012, Pages 9581-9591

  Oshaben, Kaylyn M ^a   Salari, Reza ^a   McCaslin, Darrell R ^b   Chong, Lillian T ^a   Horne, W Seth ^a  

^a UNIVERSITY OF PITTSBURGH   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COILED COIL; COILED-COIL DOMAINS; COILED-COIL PROTEINS; DIMERIZATION DOMAIN; EXPERIMENTAL CONDITIONS; FOLDED STATE; FOLDING BEHAVIOR; HELICAL FOLDING; HIGH RESOLUTION; HIGH RESOLUTION CRYSTAL STRUCTURE; LEUCINE ZIPPERS; MODEL SYSTEM; MOLECULAR DYNAMICS SIMULATIONS; PARALLEL TEMPERING; PREDICTIVE ALGORITHMS; TIME-SCALES; WILD TYPES; YEAST TRANSCRIPTION;

AMINO ACIDS; MOLECULAR DYNAMICS; OLIGOMERIZATION; TRANSCRIPTION FACTORS;

DIMERS;

TRANSCRIPTION FACTOR GCN4;

ARTICLE; BASIC LEUCINE ZIPPER MOTIF; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; MOLECULAR DYNAMICS; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; WILD TYPE;

AMINO ACID SEQUENCE; BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS; CRYSTALLOGRAPHY, X-RAY; MOLECULAR DYNAMICS SIMULATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84870210079     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301132k     Document Type: Article

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