Functional impact of polar and acidic substitutions in the lactose repressor hydrophobic monomer · monomer interface with a buried lysine

Biochemistry

Volumn 48, Issue 6, 2009, Pages 1305-1314

  Zhan, Hongli ^a,b   Sun, Zhifei ^a   Matthews, Kathleen Shive ^a  

^a RICE UNIVERSITY   (United States)

^b UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; BURIED CHARGES; CHARGED RESIDUES; CONFORMATIONAL CHANGES; DRIVING FORCES; FUNCTIONAL CHANGES; FUNCTIONAL PROPERTIES; HYDROPHOBIC INTERACTIONS; HYDROPHOBIC MONOMERS; ION-PAIR FORMATIONS; ION-PAIR INTERACTIONS; LYSINE SIDE CHAINS; MONOMER-MONOMER INTERFACES; POSITIVE CHARGES; PROTEIN STABILITIES; SALT BRIDGES; SIDE CHAINS; STRUCTURAL STABILIZATIONS;

AMIDES; AMINO ACIDS; MONOMERS; SUGARS;

HYDROPHOBICITY;

LACTOSE; LYSINE; MONOMER; REPRESSOR PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; HYDROPHOBICITY; ION PAIR CHROMATOGRAPHY; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMINO ACID SUBSTITUTION; AMINO ACIDS, ACIDIC; BACTERIAL PROTEINS; DNA, BACTERIAL; FLUORESCENCE; HYDROPHOBICITY; ISOPROPYL THIOGALACTOSIDE; LYSINE; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; OPERATOR REGIONS, GENETIC; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN SUBUNITS; REPRESSOR PROTEINS; UREA;

EID: 63749117665     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801357f     Document Type: Article

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