Alteration of hydrogen bonding in the vicinity of histidine 48 disrupts millisecond motions in RNase A

Biochemistry

Volumn 50, Issue 10, 2011, Pages 1723-1730

  Doucet, Nicolas ^a,c   Khirich, Gennady ^a   Kovrigin, Evgenii L ^b   Loria, J Patrick ^a  

^a YALE UNIVERSITY   (United States)

^b MEDICAL COLLEGE OF WISCONSIN   (United States)

^c UNIVERSITÉ LAVAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINO ACID RESIDUES; CATALYTIC FUNCTIONS; CATALYTIC SITES; CATALYTIC TURNOVER; CONFORMATIONAL EXCHANGE; DISPERSION STUDIES; DYNAMICAL FEATURES; ENZYME SYSTEMS; H-BONDING INTERACTION; H-BONDING NETWORKS; HYDROGEN BONDING INTERACTIONS; HYDROGEN BONDINGS; NMR LINE SHAPE ANALYSIS; NUCLEAR MAGNETIC RESONANCE CHEMICAL SHIFTS; PROTEIN MOTION; RNASE A; TIME-SCALES;

AMINO ACIDS; CHEMICAL ANALYSIS; CONFORMATIONS; ENZYMES; HYDROGEN; NUCLEAR MAGNETIC RESONANCE; RESONANCE;

HYDROGEN BONDS;

ALANINE; HISTIDINE; HISTIDINE 48; RIBONUCLEASE A; THREONINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYMOLOGY; ESCHERICHIA COLI; HYDROGEN BOND; MOTION; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION;

ANIMALS; CATTLE; HISTIDINE; HYDROGEN BONDING; LIGANDS; MODELS, MOLECULAR; MUTATION; RIBONUCLEASE, PANCREATIC; TIME FACTORS;

EID: 79952379799     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1018539     Document Type: Article

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