Effects of Amino Acid φ,ψ Propensities and Secondary Structure Interactions in Modulating Hα Chemical Shifts in Peptide and Protein β-Sheet
- 16 November 2001
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 123 (49) , 12318-12324
- https://doi.org/10.1021/ja0116369
Abstract
H alpha chemical shifts are often used as indicators of secondary structure formation in protein structural analysis and peptide folding studies. On the basis of NMR analysis of model beta-sheet and alpha-helical peptides, together with a statistical analysis of protein structures for which NMR data are available, we show that although the gross pattern of H alpha chemical shifts reflects backbone torsion angles, longer range effects from distant amino acids are the dominant factor determining experimental chemical shifts in beta-sheets of peptides and proteins. These show context-dependent variations that aid structural assignment and highlight anomalous shifts that may be of structural significance and provide insights into beta-sheet stability.Keywords
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