Theoretical studies on solvation contribution to the thermodynamic stability of mutants of lysozyme T4

Protein Engineering

Volumn 16, Issue 6, 2003, Pages 415-422

  Deep, Shashank ^a,b   Ahluwalia, J C ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

^b UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

Atomic solvation parameter sets; Chain free energy; Free energy of solvation of folding; Hydrogen bonding; Solvent accessible surface area

Indexed keywords

ARGININE; ASPARAGINE; ASPARTIC ACID; CYSTEINE; GLUTAMIC ACID; GLYCINE; HISTIDINE; ISOLEUCINE; LEUCINE; LYSOZYME; LYSOZYME T4; MUTANT PROTEIN; PHENYLALANINE; SERINE; THREONINE; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE; CALCULATION; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; COMPUTER SIMULATION; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; HYDROGEN BOND; MOLECULAR STABILITY; MUTATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN FOLDING; SOLVATION; THEORETICAL MODEL; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0041765690     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzg050     Document Type: Article

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