Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography

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

Volumn 111, Issue 51, 2014, Pages 18225-18230

  Wan, Qun ^a,b   Bennett, Brad C ^c   Wilson, Mark A ^d   Kovalevsky, Andrey ^e   Langan, Paul ^e   Howell, Elizabeth E ^f   Dealwis, Chris ^g  

^a Jiangsu Key Laboratory of Integrated Traditional Chinese   (China)

^b YANGZHOU UNIVERSITY   (China)

^c UNIVERSITY OF VIRGINIA   (United States)

^d UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^e OAK RIDGE NATIONAL LABORATORY   (United States)

^f UNIVERSITY OF TENNESSEE   (United States)

^g CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Deuterium exchange; Enzyme catalysis; Neutron diffraction; Protein dynamics; Protonation state

Indexed keywords

AMIDE; DIHYDROFOLATE REDUCTASE; FOLIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; WATER;

ARTICLE; ATOM; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ELECTRON; ENZYME MECHANISM; ESCHERICHIA COLI; HYDROGEN BOND; MEMBRANE STABILIZATION; NEUTRON; NEUTRON DIFFRACTION; NONHUMAN; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON TRANSPORT; STRUCTURE ANALYSIS; TAUTOMER; TAUTOMERIZATION; X RAY CRYSTALLOGRAPHY; CHEMISTRY; METABOLISM;

ESCHERICHIA COLI;

CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; NEUTRONS; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 84919941276     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1415856111     Document Type: Article

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