Peptide/protein structure analysis using the chemical shift index method: upfield alpha-CH values reveal dynamic helices and alpha L sites.

N H Andersen; B Cao; C Chen

doi:10.1016/0006-291x(92)90691-d

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Peptide/protein structure analysis using the chemical shift index method: upfield alpha-CH values reveal dynamic helices and alpha L sites.

N H Andersen·B Cao·C Chen

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Abstract

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.

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Amino Acid Sequence Antimicrobial Cationic Peptides Endothelins Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptides Plant Lectins Plant Proteins Protein Conformation Sequence Homology, Nucleic Acid Comparative Study Journal Article Research Support, Non-U.S. Gov't

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N H Andersen, B Cao, C Chen. 1992-04-30. Peptide/protein structure analysis using the chemical shift index method: upfield alpha-CH values reveal dynamic helices and alpha L sites.. https://doi.org/10.1016/0006-291x(92)90691-d

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