Energetic basis of uncoupling folding from binding for an intrinsically disordered protein

Journal of the American Chemical Society

Volumn 135, Issue 4, 2013, Pages 1288-1294

  Drobnak, Igor ^a,d   De Jonge, Natalie ^b,c,e   Haesaerts, Sarah ^b,c   Vesnaver, Gorazd ^a   Loris, Remy ^b,c   Lah, Jurij ^a  

^a UNIVERSITY OF LJUBLJANA   (Slovenia)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^d UNIVERSITY OF NOTRE DAME   (United States)

^e ArGEN X BVBA   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; BINDING AFFINITIES; BINDING PARTNERS; BINDING PROPERTIES; DESOLVATION; DISORDERED PROTEINS; FOLDED STRUCTURES; INTERMOLECULAR CONTACTS; INTERMOLECULAR INTERACTIONS; INTRAMOLECULAR INTERACTIONS; MOLECULAR FORCES; MOLECULAR TARGETS; NATIVE STATE; SPECIFIC BINDING; STRUCTURAL STUDIES; THERMODYNAMIC DATA; THREE-DIMENSIONAL STRUCTURE;

AMINO ACIDS; BINDING ENERGY;

PROTEINS;

ANTITOXIN; DNA TOPOISOMERASE (ATP HYDROLYSING); INTRINSICALLY DISORDERED PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; ENTROPY; MOLECULAR INTERACTION; MOLECULAR MODEL; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; THERMODYNAMICS;

BINDING SITES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; THERMODYNAMICS;

EID: 84873859687     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja305081b     Document Type: Article

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