Comparison of isotopic substitution methods for equilibrium and t-jump infrared studies of beta-hairpin peptide conformation.

Laser-induced temperature jump (T-jump) kinetics of relaxation was measured by absorbance of infrared (IR) detection for a set of peptide beta-hairpin, associated with hairpins Trpzip2, but it contains a label isotope single, (13) C to the amide C horizontal Lineo residue the selected both at the center and in the terminal strands of the hairpin. Variation in the behavior of a single labeled peptide compared with those previously reported for the double-la

beled variants. Although a single label does not produce an increase in spectral intensity, as seen to the labeling of cross-strand, IR frequency shift hairpin diagnostic still ongoing. If C horizontal Lineo at the beta-strands of the hairpin (between residues Trp) is labeled, the dynamic behavior of the local fashion similar to the results obtained with the double label in terms of the relaxation time and energy and closely track the kinetics of activation of beta-strand component.

This means that both the property, local secondary structure (change varphi, psi), or cross-strand clutch is activated by the formation of H-bonded strands and loosening with the same kinetic mechanism. Single residue at position terminal label have different behaviors and less able to detect because it overlaps with the component (12) C, in contrast with the double label involving the position, which is enhanced due to coupling. DFT-based spectral simulation using NMR structure of Trpzip2C showed that single-labeled peptides must have a roughly equivalent (12) C band but (13) C mode frequency will vary with the position of the sequence. effective solvent correction using COSMO yield significant changes in frequency but not in relative isotope shift in the spectrum obtained we calculated. The sequence dependency label position is shown to be more discriminatory than the variation thermodynamics kinetics change.


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