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Volumn 10, Issue 9, 2001, Pages 1822-1834
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Influence of Glu-376 → Gln mutation on enthalpy and heat capacity changes for the binding of slightly altered ligands to medium chain acyl-CoA dehydrogenase
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Author keywords
2 Azaoctanoyl CoA; Glu 376 Gln mutation; Isothermal microcalorimetry; Medium chain acyl CoA dehydrogenase; Octenoyl CoA; Thermodynamics of ligand binding
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Indexed keywords
MEDIUM CHAIN ACYL COENZYME A DEHYDROGENASE;
AMINO ACID SUBSTITUTION;
ARTICLE;
ELECTRICITY;
ENTHALPY;
ENTROPY;
ENZYME ACTIVE SITE;
ENZYME BINDING;
ENZYME SPECIFICITY;
HEAT TOLERANCE;
LIGAND BINDING;
MICROCALORIMETRY;
MOLECULAR MODEL;
PRIORITY JOURNAL;
PROTEIN PROTEIN INTERACTION;
PROTEIN STRUCTURE;
TEMPERATURE DEPENDENCE;
THERMODYNAMICS;
ACYL COENZYME A;
ACYL-COA DEHYDROGENASE;
ACYL-COA DEHYDROGENASES;
ANIMALS;
CALORIMETRY;
GLUTAMIC ACID;
GLUTAMINE;
HUMANS;
LIGANDS;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PROTEIN BINDING;
SOLVENTS;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
SWINE;
TEMPERATURE;
THERMODYNAMICS;
WATER;
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EID: 0034842061
PISSN: 09618368
EISSN: None
Source Type: Journal
DOI: 10.1110/ps.51401 Document Type: Article |
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Times cited : (11)
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References (75)
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