SIMPLE estimate of the free energy change due to aliphatic mutations: Superior predictions based on first principles

Proteins: Structure, Function and Genetics

Volumn 68, Issue 4, 2007, Pages 850-862

  Bueno, Marta ^a,b   Camacho, Carlos J ^a   Sancho, Javier ^a,b  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ZARAGOZA   (Spain)

Author keywords

Hydrophobic effect; Protein folding; Protein stability; Stability prediction; Van der Waals interactions

Indexed keywords

ALIPHATIC COMPOUND; MUTANT PROTEIN; SOLVENT;

ACCURACY; ARTICLE; BIOINFORMATICS; ELECTRICITY; ENERGY ABSORPTION; ENTROPY; HYDROPHOBICITY; MUTATIONAL ANALYSIS; PARAMETER; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; SOLUTE; THERMODYNAMICS;

COMPUTATIONAL BIOLOGY; ENZYMES; MODELS, GENETIC; MODELS, THEORETICAL; MUTATION; PROTEINS; REPRODUCIBILITY OF RESULTS; SOLVENTS; THERMODYNAMICS;

EID: 34548746885     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21453     Document Type: Article

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