13C Isotope Labeling of Hydrophobic Peptides. Origin of the Anomalous Intensity Distribution in the Infrared Amide I Spectral Region of β-Sheet Structures
- 12 January 2000
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (4) , 677-683
- https://doi.org/10.1021/ja992522o
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
- Ab initio simulations of the vibrational circular dichroism of coupled peptidesJournal of the American Chemical Society, 1993
- Potential of carbon-13 and nitrogen-15 labeling for studying protein-protein interactions using Fourier-transform infrared spectroscopyBiochemistry, 1992
- Model calculations on the amide-I infrared bands of globular proteinsThe Journal of Chemical Physics, 1992
- Location of .beta.-sheet-forming sequences in amyloid proteins by FTIRJournal of the American Chemical Society, 1991
- Isotopically enhanced infrared spectroscopy: a novel method for examining secondary structure at specific sites in conformationally heterogeneous peptidesJournal of the American Chemical Society, 1991
- The Infrared Spectra of Polypeptides in Various Conformations: Amide I and II Bands1Journal of the American Chemical Society, 1961
- Perturbation Treatment of the Characteristic Vibrations of Polypeptide Chains in Various ConfigurationsThe Journal of Chemical Physics, 1960