The pH-dependence of amide chemical shift of Asp/Glu reflects its pKa in intrinsically disordered proteins with only local interactions

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 7, 2006, Pages 1227-1233

  Pujato, Mario ^a   Navarro, Abel ^a   Versace, Rodney ^a   Mancusso, Romina ^a   Ghose, Ranajeet ^a   Tasayco, María Luisa ^a  

^a CITY COLLEGE OF NEW YORK   (United States)

Author keywords

Nuclear magnetic resonance; pKa; Unfolded state of proteins

Indexed keywords

ASPARTIC ACID; CARBOXYLIC ACID; GLUTAMIC ACID;

ARTICLE; COMPARATIVE STUDY; ELECTRICITY; MOLECULAR INTERACTION; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; TITRIMETRY;

AMIDES; AMINO ACID SEQUENCE; ASPARTIC ACID; ELECTROSTATICS; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; THIOREDOXIN;

EID: 33746047069     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.04.014     Document Type: Article

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