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Volumn 39, Issue 47, 2000, Pages 14448-14456
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Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions
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Author keywords
[No Author keywords available]
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Indexed keywords
ALANINE;
AMINO ACID;
GLYCINE;
ISOLEUCINE;
LEUCINE;
LYSOZYME;
METHIONINE;
MUTANT PROTEIN;
PHENYLALANINE;
VALINE;
ARTICLE;
CRYSTAL STRUCTURE;
ENZYME CONFORMATION;
ENZYME DENATURATION;
ENZYME STABILITY;
HYDRATION;
HYDROGEN BOND;
HYDROPHOBICITY;
PRIORITY JOURNAL;
SURFACE PROPERTY;
THERMODYNAMICS;
ALANINE;
AMINO ACID SUBSTITUTION;
AMINO ACIDS;
CALORIMETRY, DIFFERENTIAL SCANNING;
CRYSTALLOGRAPHY, X-RAY;
ENZYME STABILITY;
GLYCINE;
HUMANS;
ISOLEUCINE;
LEUCINE;
MEMBRANE PROTEINS;
METHIONINE;
MURAMIDASE;
MUTAGENESIS, SITE-DIRECTED;
PHENYLALANINE;
PROTEIN CONFORMATION;
THERMODYNAMICS;
VALINE;
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EID: 0034727682
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0015717 Document Type: Article |
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Times cited : (39)
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References (51)
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