Surface salt bridges, double-mutant cycles, and protein stability: An experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein L9

Biochemistry

Volumn 42, Issue 23, 2003, Pages 7050-7060

  Luisi, Donna L ^a,c   Snow, Christopher D ^c,d   Lin, Jo Jin ^a   Hendsch, Zachary S ^b   Tidor, Bruce ^b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b Massachusetts Inst of Technology ^*  (United States)

^c PFIZER INC   (United States)

^d STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; COMPUTATION THEORY; ELECTROSTATICS; ENTROPY; FREE ENERGY;

DOUBLE-MUTANT CYCLES;

PROTEINS;

ALANINE; ASPARAGINE; ASPARTIC ACID; NITRILE; RIBOSOMAL PROTEIN L9; RIBOSOME PROTEIN; SOLVENT; UNCLASSIFIED DRUG;

ACIDITY; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CALCULATION; CIRCULAR DICHROISM; ELECTRIC POTENTIAL; ENERGY; ENTROPY; GEOMETRY; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; ASPARTIC ACID; CIRCULAR DICHROISM; ELECTROSTATICS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; RIBOSOMAL PROTEINS; SOLVENTS; THERMODYNAMICS; UREA;

EID: 0038131734     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027202n     Document Type: Article

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