Design of a fluorescence polarization assay platform for the study of human Hsp70.
The 70kDa heat shock proteins (Hsp70) are molecular chaperones that assist in folding of newly synthesized polypeptides, refolding or denaturation of misfolded proteins, and translocation of proteins across biological membranes. In addition, Hsp70 play regulatory roles in signal transduction, cell cycle, and apoptosis. Here, we present a novel assay platform based on fluorescence polarization that is suitable for investigating the yet elusive molecular mechanics of human Hsp70 allosteric regulation.
Program in Molecular Pharmacology and Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Yanlong
Y
Kang
Tony
T
Taldone
Cristina C
CC
Clement
Sheara W
SW
Fewell
Julia
J
Aguirre
Jeffrey L
JL
Brodsky
Gabriela
G
Chiosis
D000495:Allosteric Site; D017209:Apoptosis; D002462:Cell Membrane / Q000378:metabolism; D003198:Computer Simulation; D004305:Dose-Response Relationship, Drug; D005454:Fluorescence Polarization / Q000295:instrumentation*; D005456:Fluorescent Dyes / Q000494:pharmacology*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D018832:Molecular Chaperones / Q000737:chemistry; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D015398:Signal Transduction; D013050:Spectrometry, Fluorescence / Q000295:instrumentation / Q000379:methods*
D005456:Fluorescent Dyes; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D010455:Peptides