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Comparison of Isotopic substitution methods for equilibrium and T-Jump infrared studies of beta-Hairpin Peptide conformation

Comparison of Isotopic substitution methods for equilibrium and T-Jump infrared studies of beta-Hairpin Peptide conformation

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HAUSER, Karin, Oliver RIDDERBUSCH, Anjan ROY, Alexandra HELLERBACH, Rong HUANG, Timothy A. KEIDERLING, 2010. Comparison of Isotopic substitution methods for equilibrium and T-Jump infrared studies of beta-Hairpin Peptide conformation. In: The Journal of Physical Chemistry B. 114(35), pp. 11628-11637. ISSN 1520-6106. eISSN 1520-5207

@article{Hauser2010-09-09Compa-12597, title={Comparison of Isotopic substitution methods for equilibrium and T-Jump infrared studies of beta-Hairpin Peptide conformation}, year={2010}, doi={10.1021/jp1028245}, number={35}, volume={114}, issn={1520-6106}, journal={The Journal of Physical Chemistry B}, pages={11628--11637}, author={Hauser, Karin and Ridderbusch, Oliver and Roy, Anjan and Hellerbach, Alexandra and Huang, Rong and Keiderling, Timothy A.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/12597"> <dc:language>eng</dc:language> <dcterms:title>Comparison of Isotopic substitution methods for equilibrium and T-Jump infrared studies of beta-Hairpin Peptide conformation</dcterms:title> <dc:creator>Hellerbach, Alexandra</dc:creator> <dc:contributor>Hauser, Karin</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-06-16T08:33:50Z</dcterms:available> <dc:creator>Keiderling, Timothy A.</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/12597"/> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:contributor>Keiderling, Timothy A.</dc:contributor> <dc:contributor>Ridderbusch, Oliver</dc:contributor> <dc:creator>Huang, Rong</dc:creator> <dc:creator>Ridderbusch, Oliver</dc:creator> <dc:contributor>Huang, Rong</dc:contributor> <dcterms:issued>2010-09-09</dcterms:issued> <dc:creator>Hauser, Karin</dc:creator> <dc:contributor>Hellerbach, Alexandra</dc:contributor> <dc:rights>deposit-license</dc:rights> <dcterms:bibliographicCitation>First publ. in: Journal of Physical Chemistry : B ; 114 (2010), 35. - S. 11628-11637</dcterms:bibliographicCitation> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-06-16T08:33:50Z</dc:date> <dc:creator>Roy, Anjan</dc:creator> <dc:contributor>Roy, Anjan</dc:contributor> <dcterms:abstract xml:lang="eng">Laser induced temperature jump (T-jump) relaxation kinetics were measured with infrared absorbance (IR) detection for a set of β-hairpin peptides, related to the Trpzip2 hairpin, but containing single isotopic labels, 13C on the amide C═O of selected residues both in the center of the strands and at the terminal regions of the hairpin. Variations in the behavior of single labeled peptides are compared to those previously reported for double labeled variants. Although single labels do not result in spectral intensity enhancement, as seen for cross-strand labeling, the IR frequency shifts are still diagnostic of hairpin unfolding. If C═O’s in the β-strand portion of the hairpin (between the Trp residues) are labeled, the dynamic behavior of the local modes is similar to the results obtained with double labels in terms of relaxation time and activation energy and closely tracks the kinetics of the β-strand components. This implies that either property, local secondary structure (change of ,ψ), or cross-strand coupling enabled by strand formation and H-bonding relaxes with the same kinetic mechanism. Single labeled residues on the terminal positions have a different behavior and are less able to be detected due to overlap with the 12C components, in contrast to double labels involving these positions, which are enhanced due to coupling. DFT-based spectral simulations that use the NMR structure of Trpzip2C indicate that the single labeled peptides should have roughly equivalent 12C bands but the 13C mode frequencies will vary with sequence position. Effective solvent corrections using COSMO yield significant changes in the frequencies but not in the relative isotope shifts obtained in our calculated spectra. Sequence positional dependence of labels is shown to be more discriminatory for kinetics changes than for thermodynamic variations.</dcterms:abstract> </rdf:Description> </rdf:RDF>

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