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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.
Lipid-induced conformational transitions of β-lactoglobulin
It is shown that the tertiary structure of lipid-bound βLG is highly expanded but not completely disrupted, and the degree of induced α-helix depends on the lipid concentration and is strongly affected by the charge of the protein and lipids as well as the ionic strength of the solution.
Nature of vibrational coupling in helical peptides: an isotopic labeling study.
- Rong Huang, J. Kubelka, W. Barber-Armstrong, R. A. Silva, S. Decatur, T. Keiderling
- ChemistryJournal of the American Chemical Society
- 10 February 2004
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.
Conformational transitions in phosvitin with pH variation. Vibrational circular dichroism study.
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.
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-,…
Transfer of molecular property tensors in cartesian coordinates: A new algorithm for simulation of vibrational spectra
The results for model calculations of the force field and vibrational frequencies for N-methylacetamide show that the method removes errors associated with numerical artifacts caused by nonlinearity of the otherwise required Cartesian to internal coordinate transformation.
Relationship between hydrophobic interactions and secondary structure stability for Trpzip beta-hairpin peptides.
- T. Takekiyo, Ling Wu, Y. Yoshimura, A. Shimizu, T. Keiderling
- Chemistry, BiologyBiochemistry
- 24 February 2009
Comparison of conformational transitions monitored by CD and IR reveals them to have multistate behavior in which the temperature-induced disruption of the Trp-Trp interaction (tertiary structure) occurs at a lower temperature than the unfolding of the secondary structure.
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.
Cross-strand coupling and site-specific unfolding thermodynamics of a trpzip beta-hairpin peptide using 13C isotopic labeling and IR spectroscopy.
- Rong Huang, Ling Wu, D. McElheny, P. Bouř, Anjan Roy, T. Keiderling
- ChemistryThe journal of physical chemistry. B
- 23 April 2009
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.