Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 → His

Protein Science

Volumn 18, Issue 5, 2009, Pages 863-870

  Mooers, Blaine H M ^a,b   Tronrud, Dale E ^a,c   Matthews, Brian W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

^c OREGON STATE UNIVERSITY   (United States)

Author keywords

Bond angle strain; Full matrix refinement; Rotamer strain; T4 lysozyme; Temperature sensitive mutant

Indexed keywords

ARGININE; HISTIDINE; LYSOZYME; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE T4; CONFORMATION; CRYSTAL; CRYSTAL STRUCTURE; GEOMETRY; HYDROGEN BOND; MUTATION; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE SENSITIVE MUTANT; WILD TYPE; X RAY CRYSTALLOGRAPHY;

BACTERIOPHAGE T4; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN BONDING; MODELS, MOLECULAR; MURAMIDASE; MUTATION; TEMPERATURE; VIRAL PROTEINS;

EID: 65649094471     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.93     Document Type: Article

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