Effect of pH, urea, peptide length, and neighboring amino acids on alanine α-proton random coil chemical shifts

Biopolymers

Volumn 85, Issue 1, 2007, Pages 72-80

  Carlisle, Elizabeth A ^a   Holder, Jessica L ^a   Maranda, Abby M ^a   De Alwis, Adamberage R ^a   Selkie, Ellen L ^a   McKay, Sonya L ^a  

^a DENISON UNIVERSITY   (United States)

Author keywords

proton; Amino acid; Chemical shift; NMR; Peptides; Random coil

Indexed keywords

AROMATIC COMPOUNDS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PH EFFECTS; PROTEINS; UREA;

Α-PROTON; CHEMICAL SHIFT; CHEMICAL SHIFT INDEX (CSI); PEPTIDES; RANDOM COIL;

AMINO ACIDS;

ALANINE; HISTIDINE; LEUCINE; PHENYLALANINE; PROLINE; TRYPTOPHAN; TYROSINE; UREA; VALINE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONCENTRATION RESPONSE; PH MEASUREMENT; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

ALANINE; AMINO ACID SEQUENCE; AMINO ACIDS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTONS; REFERENCE STANDARDS; UREA;

EID: 33846488586     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20614     Document Type: Article

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