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Volumn 64, Issue 4, 2002, Pages 210-220
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Importance of mutant position in ramachandran plot for predicting protein stability of surface mutations
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Author keywords
Amino acid properties; Protein stability; Ramachandran plot; Sequence and structural effects; Surface mutants; Unfolding free energy change
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Indexed keywords
AMINO ACIDS;
CONFORMATIONS;
ENTROPY;
HYDRATION;
HYDROPHOBICITY;
MOLECULAR BIOLOGY;
MUTAGENESIS;
STRAIN ENERGY;
PROTEINS;
AMINO ACID;
MUTANT PROTEIN;
PROTEIN;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
ENERGY;
HYDROPHOBICITY;
MOLECULAR SIZE;
MUTATIONAL ANALYSIS;
PHYSICAL CHEMISTRY;
PREDICTION;
PROTEIN CONFORMATION;
PROTEIN ENGINEERING;
PROTEIN FOLDING;
PROTEIN FUNCTION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
SEQUENCE ANALYSIS;
STRUCTURE ANALYSIS;
BIOPOLYMERS;
DRUG STABILITY;
HYDROGEN BONDING;
MUTATION;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, SECONDARY;
PROTEINS;
THERMODYNAMICS;
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EID: 0037025821
PISSN: 00063525
EISSN: None
Source Type: Journal
DOI: 10.1002/bip.10125 Document Type: Article |
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Times cited : (43)
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References (37)
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