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Volumn 37, Issue 50, 1998, Pages 17537-17544
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The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus: Equilibrium and kinetic studies of guanidine hydrochloride- induced unfolding and refolding
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Author keywords
[No Author keywords available]
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Indexed keywords
ARTICLE;
CONFORMATIONAL TRANSITION;
ENZYME CONFORMATION;
ENZYME KINETICS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN FOLDING;
PYROCOCCUS;
CIRCULAR DICHROISM;
DOSE-RESPONSE RELATIONSHIP, DRUG;
ENZYME STABILITY;
GUANIDINE;
HEAT;
KINETICS;
PROTEIN FOLDING;
PYROCOCCUS FURIOSUS;
PYROGLUTAMYL-PEPTIDASE I;
THERMODYNAMICS;
ARCHAEA;
BACILLUS AMYLOLIQUEFACIENS;
BACTERIA (MICROORGANISMS);
PYROCOCCUS;
PYROCOCCUS FURIOSUS;
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EID: 0032534842
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi9814585 Document Type: Article |
Times cited : (50)
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References (7)
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