Denaturation of an extremely stable hyperthermophilic protein occurs via a dimeric intermediate

Extremophiles

Volumn 11, Issue 1, 2007, Pages 179-189

  Powers, Sara Lawrence ^a   Robinson, Clifford R ^b   Robinson, Anne Skaja ^a  

^a University of Delaware   (United States)

^b UNIVERSITY OF DELAWARE   (United States)

Author keywords

Glucosidase; Archaea; CelB; Determinants of stability; Hyperthermophile; Oligomerization; Pyrococcus furiosus; Tetramer

Indexed keywords

ARCHAEAL PROTEIN; BETA GLUCOSIDASE; GUANIDINE; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; UREA;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; ENZYME STABILITY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR CLONING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PYROCOCCUS FURIOSUS; SPECTROFLUOROMETRY; TEMPERATURE;

ARCHAEAL PROTEINS; BETA-GLUCOSIDASE; CIRCULAR DICHROISM; CLONING, MOLECULAR; DIMERIZATION; ENZYME STABILITY; GUANIDINE; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; PYROCOCCUS FURIOSUS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; UREA;

ARCHAEA; PYROCOCCUS FURIOSUS;

EID: 33846176929     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-006-0030-5     Document Type: Article

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