An exceptionally stable Group II chaperonin from the hyperthermophile Pyrococcus furiosus

Archives of Biochemistry and Biophysics

Volumn 486, Issue 1, 2009, Pages 12-18

  Luo, Haibin ^a   Laksanalamai, Pongpan ^a   Robb, Frank T ^a  

^a UNIVERSITY OF MARYLAND   (United States)

Author keywords

ATPase activity; Chaotrope; Cpn; Hsp60; Protein refolding; sHsp; SPR

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; GUANIDINE; HEAT SHOCK PROTEIN;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; HEAT SHOCK; HYDROLYSIS; IONIC STRENGTH; LYSOSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PYROCOCCUS FURIOSUS; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

ADENOSINE TRIPHOSPHATASES; ARCHAEAL PROTEINS; BASE SEQUENCE; CHAPERONINS; CLONING, MOLECULAR; DNA PRIMERS; DRUG STABILITY; GENES, ARCHAEAL; HEAT-SHOCK PROTEINS; HOT TEMPERATURE; MURAMIDASE; PROTEIN BINDING; PROTEIN FOLDING; PYROCOCCUS FURIOSUS; RECOMBINANT PROTEINS; SURFACE PLASMON RESONANCE;

ARCHAEA; PYROCOCCUS FURIOSUS;

EID: 67349208011     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.03.005     Document Type: Article

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