The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 50, 2014, Pages 17881-17886

  Jahn, Markus ^a   Rehn, Alexandra ^a   Pelz, Benjamin ^a   Hellenkamp, Björn ^a   Richter, Klaus ^a,b   Riefa, Matthias ^a,b   Buchner, Johannes ^a,b   Hugel, Thorsten ^a,c  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b Munich Center for Integrated Protein Science   (Germany)

^c UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Asymmetric state; FRET; Hsp90 conformation; Optical tweezers; Single molecule

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90; CROSS LINKING REAGENT; HSP82 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; BIOCHEMISTRY; CONTROLLED STUDY; IN VIVO STUDY; MOLECULAR DOCKING; NONHUMAN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; CHEMICAL STRUCTURE; CHEMISTRY; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; IMMUNOBLOTTING; METABOLISM; OPTICAL TWEEZERS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN TERTIARY STRUCTURE; ULTRACENTRIFUGATION; WESTERN BLOTTING;

BLOTTING, WESTERN; CROSS-LINKING REAGENTS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HSP90 HEAT-SHOCK PROTEINS; IMMUNOBLOTTING; MODELS, MOLECULAR; OPTICAL TWEEZERS; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS; ULTRACENTRIFUGATION;

EID: 84918567953     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1414073111     Document Type: Article

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