A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

EMBO Journal

Volumn 16, Issue 3, 1997, Pages 659-671

  Lee, Garrett J ^a   Roseman, Alan M ^b   Saibil, Helen R ^b   Vierling, Elizabeth ^a  

^a University of Arizona   (United States)

^b UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

Heat denaturation; Molecular chaperone; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN; LUCIFERASE; MALATE DEHYDROGENASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENZYME SUBSTRATE COMPLEX; GEL PERMEATION CHROMATOGRAPHY; GENETIC CONSERVATION; HYDROPHOBICITY; NONHUMAN; PEA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FOLDING; RABBIT; RETICULOCYTE; TEMPERATURE; WHEAT GERM;

AMINO ACID SEQUENCE; ANILINO NAPHTHALENESULFONATES; ANIMALS; CHROMATOGRAPHY, GEL; CITRATE (SI)-SYNTHASE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORESCENT DYES; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HEAT-SHOCK PROTEINS; IMMUNOGLOBULIN G; LUCIFERASES; MALATE DEHYDROGENASE; MICROSCOPY, ELECTRON; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PEAS; PEPTIDE FRAGMENTS; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SCATTERING, RADIATION; SEQUENCE ANALYSIS; TEMPERATURE;

ORYCTOLAGUS CUNICULUS; PISUM SATIVUM; TRITICUM AESTIVUM;

EID: 0031024691     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.3.659     Document Type: Article

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