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Volumn 61, Issue 4, 1997, Pages 411-418

Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study

(4) Csermely, Péter b Miyata, Yoshihiko a Soti, Csaba b Yahara, Ichiro a

a TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE (Japan)

b SEMMELWEIS UNIVERSITY (Hungary)

Author keywords

Calmodulin; Casein; Histones; hsp90; Molecular chaperones; Surface plasmon resonance

Indexed keywords

CALMODULIN; CASEIN; HEAT SHOCK PROTEIN 90; HISTONE H1;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DISSOCIATION CONSTANT; HYDROPHOBICITY; MALE; MOUSE; NONHUMAN; PH; PROTEIN BINDING; PROTEIN STRUCTURE; RAT; SPECTROFLUOROMETRY; SURFACE CHARGE;

ADENOSINE TRIPHOSPHATE; BIOSENSING TECHNIQUES; CALMODULIN; CASEINS; CHEMISTRY, PHYSICAL; HISTONES; HSP90 HEAT-SHOCK PROTEINS; PROTEIN BINDING; SURFACE PROPERTIES;

ANIMALIA;

EID: 0030802135 PISSN: 00243205 EISSN: None Source Type: Journal
DOI: 10.1016/S0024-3205(97)00398-6 Document Type: Article

Times cited : (23)

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