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.
Kang
Yanlong
Y
Program in Molecular Pharmacology and Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Taldone
Tony
T
Clement
Cristina C
CC
Fewell
Sheara W
SW
Aguirre
Julia
J
Brodsky
Jeffrey L
JL
Chiosis
Gabriela
G
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