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The anomalous infrared amide I intensity distribution in (13)C isotopically labeled peptide beta-sheets comes from extended, multiple-stranded structures: an ab initio study.
The results demonstrate that the anomalous intensity previously reported for the isotopically shifted amide I in (13)C labeled peptides is due to formation of multistranded beta-sheet structures in this conformation. Expand
Lipid-induced conformational transitions of β-lactoglobulin
Bovine β-lactoglobulin (βLG) provides an excellent model protein system for β-to-α conformational change, but its behavior varies when the change is induced by alcohols, surfactants, or lipidExpand
Statistical analyses of the vibrational circular dichroism of selected proteins and relationship to secondary structures.
These statistical analyses represent the first determination of a quantitative relationship between VCD spectra and secondary structure in proteins. Expand
Reassessment of the random coil conformation: Vibrational CD study of proline oligopeptides and related polypeptides
It is concluded that the “random coil” conformation has a large fraction of helical regions, conformationally similar to the left‐handed, 31 polyproline II helix, as was previously suggested by Krimm and co‐workers. Expand
Differentiation of β-Sheet-Forming Structures: Ab Initio-Based Simulations of IR Absorption and Vibrational CD for Model Peptide and Protein β-Sheets
Ab initio quantum mechanical computations of force fields (FF) and atomic polar and axial tensors (APT and AAT) were carried out for triamide strands Ac-A-A-NH-CH3 clustered into single-, double-,Expand
Transfer of molecular property tensors in cartesian coordinates: A new algorithm for simulation of vibrational spectra
A direct transfer of Cartesian molecular force fields (FF) and electric property tensors is tested on model systems and compared to transfer in internal coordinates with an aim to improve simulationExpand
Nature of vibrational coupling in helical peptides: an isotopic labeling study.
Infrared and vibrational circular dichroism spectra measured for a series of isotopically labeled, 25 residue, alpha-helical peptides of the sequence Ac-(AAAAK)(4)AAAAY-NH(2) confirmed the utility of isotopic labels for site-specific structural studies with vibrational spectra. Expand
Characterization of alanine-rich peptides, Ac-(AAKAA)n-GY-NH2 (n = 1-4), using vibrational circular dichroism and Fourier transform infrared. Conformational determination and thermal unfolding.
Vibrational circular dichroism and Fourier transform IR data were measured for a series of short alanine-based peptides, indicating increased helical stability at higher concentrations and consistent with lower-concentration electronic CD results. Expand
Cross-strand coupling and site-specific unfolding thermodynamics of a trpzip beta-hairpin peptide using 13C isotopic labeling and IR spectroscopy.
This study illustrates the consequences of multistate conformational change at the residue- or sequence-specific level in a system whose structure is dominated by hydrophobic collapse. Expand
Circular dichroism and magnetic circular dichroism of iron-sulfur proteins.
The CD and MCD spectra reported provide a broader base than heretofore available for the characterization of iron-sulfur proteins containing 2-Fe and 4-Fe clusters and for the evaluation of electronic structural models for these clusters. Expand