Controlling peptide folding with repulsive interactions between phosphorylated amino acids and tryptophan

Journal of the American Chemical Society

Volumn 131, Issue 39, 2009, Pages 14081-14087

  Riemen, Alexander J ^a   Waters, Marcey L ^a  

^a The University of North Carolina at Chapel Hill   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE MUTANTS; GLUTAMIC ACID; HAIRPIN STRUCTURES; PEPTIDE FOLDING; PHOSPHATE GROUP; PHOSPHORYLATED AMINO ACID; PROTEIN STRUCTURES; REPULSIVE INTERACTIONS; TRYPTOPHAN RESIDUES;

AMINATION; AMINES; BIOLOGICAL SYSTEMS; ORGANIC ACIDS; PEPTIDES; PHOSPHORYLATION;

AMINO ACIDS;

AMINO ACID; SERINE; THREONINE; TRYPTOPHAN; TYROSINE;

ARTICLE; CHEMICAL INTERACTION; PH MEASUREMENT; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE;

CIRCULAR DICHROISM; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PHOSPHORYLATION; PHOSPHOSERINE; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SERINE; THREONINE; TRYPTOPHAN; TYROSINE;

EID: 70349614632     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9047575     Document Type: Article

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