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Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 4, 2005, Pages 1006-1011

α-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities

(4) Haddad, Kristin Coffman a Sudmeier, James L a Bachovchin, Daniel A a Bachovchin, William W a

a TUFTS UNIVERSITY SCHOOL OF MEDICINE (United States)

Author keywords

Catalytic triad; Lyophilization; Serine protease mechanism

Indexed keywords

HISTIDINE; SERINE PROTEINASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; DISSOLUTION; ENZYME ACTIVE SITE; FREEZE DRYING; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; TEMPERATURE DEPENDENCE;

CATALYSIS; FREEZE DRYING; HYDROGEN-ION CONCENTRATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES; TEMPERATURE;

BACTERIA (MICROORGANISMS);

EID: 12844286056 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.0409279102 Document Type: Article

Times cited : (26)

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