Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability

Journal of Molecular Biology

Volumn 292, Issue 5, 1999, Pages 1111-1120

  Wray, Jonathan W ^a   Baase, Walter A ^a   Lindstrom, Joel D ^a   Weaver, Larry H ^a   Poteete, Anthony R ^b   Matthews, Brian W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

Compensation; Mutagenesis; Thermal factors; Thermostability

Indexed keywords

ALANINE; GLUTAMINE; LEUCINE; LYSOZYME; MUTANT PROTEIN; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE T4; CELL WALL; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ENZYME INACTIVATION; HYDROLYSIS; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; REVERTANT; THERMODYNAMICS;

T4 BACTERIOPHAGE; UNIDENTIFIED BACTERIOPHAGE;

EID: 0033536578     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3102     Document Type: Article

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