A phosphoserine-lysine salt bridge within an α-helical peptide, the strongest α-helix side-chain interaction measured to date

Biochemistry

Volumn 44, Issue 20, 2005, Pages 7553-7558

  Errington, Neil ^a   Doig, Andrew J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PH EFFECTS; PHOSPHATES; TITRATION;

LYSINE SIDE CHAINS; PEPTIDES; PHOSPHORLYLATION; SALT BRIDGE;

PROTEINS;

BRIDGED COMPOUND; LYSINE; PHOSPHATE; PHOSPHOSERINE; SODIUM CHLORIDE;

ALPHA HELIX; ARTICLE; PH; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; LYSINE; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOSPHORYLATION; PHOSPHOSERINE; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; SALTS; SERINE; THERMODYNAMICS;

EID: 18844383462     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050297j     Document Type: Article

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