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Volumn 44, Issue 1, 2001, Pages 1-11
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Structural basis for the appearance of a molten globule state in chimeric molecules derived from lysozyme and α-lactalbumin
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Author keywords
Chimera; Human lysozyme; Hydrophobic core; Intermediate state; Molten globule; Protein unfolding
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Indexed keywords
ALPHA LACTALBUMIN;
CALCIUM ION;
CHIMERIC PROTEIN;
GLOBULAR PROTEIN;
HELIX LOOP HELIX PROTEIN;
LYSOZYME;
PROTEIN LYLA 1A;
PROTEIN LYLA 1B;
UNCLASSIFIED DRUG;
ARTICLE;
CALCIUM BINDING;
CALCIUM TRANSPORT;
CHIMERA;
ENZYME STRUCTURE;
HUMAN;
HYDROPHOBICITY;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
SACCHAROMYCES CEREVISIAE;
STRUCTURE ANALYSIS;
AMINO ACID SEQUENCE;
ANILINO NAPHTHALENESULFONATES;
ANIMALS;
CATTLE;
ENZYME ACTIVATION;
HUMANS;
HYDROGEN-ION CONCENTRATION;
LACTALBUMIN;
MURAMIDASE;
MUTAGENESIS;
PROTEIN BINDING;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN RENATURATION;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT FUSION PROTEINS;
SEQUENCE DELETION;
SUBSTRATE SPECIFICITY;
TEMPERATURE;
BOVINAE;
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EID: 0035400194
PISSN: 08873585
EISSN: None
Source Type: Journal
DOI: 10.1002/prot.1065 Document Type: Article |
Times cited : (6)
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References (67)
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