Peptide/protein structure analysis using the chemical shift index method: upfield alpha-CH values reveal dynamic helices and alpha L sites.
The alpha-CH shifts observed by 1H NMR for medium-sized peptides and for an unusual small protein, herein, which has a high density of alpha L conformations within its 43 residue length, reveal that the recently introduced chemical shift index (CSI) analysis places short dynamic helices (alpha R) and alpha L residues in the same category as stable helices. The method appears to be a promising addition to the arsenal of methods for peptide structure analysis and is clearly not limited to rigid protein systems.
Andersen
N H
NH
Department of Chemistry, University of Washington, Seattle 98195.
Cao
B
B
Chen
C
C
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D016232:Endothelins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D037121:Plant Lectins; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D023181:Antimicrobial Cationic Peptides; D016232:Endothelins; D010455:Peptides; D037121:Plant Lectins; D010940:Plant Proteins; C045875:hevein