Trpzip-Based Beta-Hairpin Equilibrium and Temperature Jump IR Studies Enhanced by Site-Specific Isotope Labeling

Huang, Rong; Krejtschi, Carsten; Hauser, Karin; Keiderling, Timothy A.

Trpzip-Based Beta-Hairpin Equilibrium and Temperature Jump IR Studies Enhanced by Site-Specific Isotope Labeling

Dateien

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Datum

2008

Autor:innen

Huang, Rong

Krejtschi, Carsten

Hauser, Karin

Keiderling, Timothy A.

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Chemie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biophysical Journal. 2008, 94(2), pp. 610-613. ISSN 0006-3495. Available under: doi: 10.1016/S0006-3495(08)79104-5

Zusammenfassung

Beta-hairpins may be the smallest folding units in a protein, and two antiparallel beta-strands connected by a turn make the simplest model system for analysis of the interactions and dynamics of betasheets. We have studied site-specific conformational dynamics by use of equilibrium and temperature-jump kinetic IR-spectroscopy with site-specific enhancement via isotopic labelling of the amide with 13C=O in isotopically labeled variants of a modification of Cochran’s 12-residue tryptophan zipper peptide, TrpZip2. Equilibrium measurements reflect decreased stability of the hairpin crossstrand H-bonds at the turn and the termini. Spectral analysis of single and doubly labeled species is used to determine specific coupling levels. 13C=O groups introduced at different amide positions lead to distinguishable cross-strand coupling of the labelled residues which is lost on unfolding. These labels have distinct frequency patterns and different thermal behaviors depending on their position in the hairpin and reflect the local structural variation along the strands. Relaxation kinetics upon laser-induced T-jumps of ~10 C have time constants of a few microsec that decrease with ncrease of the initial temperature of the peptide before the temperature jump. Analysis of the data supports a multistate folding process, consistent with the hydrophobic collapse hypothesis for hairpin folding, but it is not possible to clearly define a folding and unfolding rate.

Fachgebiet (DDC)

540 Chemie

Zitieren

ISO 690

HUANG, Rong, Carsten KREJTSCHI, Karin HAUSER, Timothy A. KEIDERLING, 2008. Trpzip-Based Beta-Hairpin Equilibrium and Temperature Jump IR Studies Enhanced by Site-Specific Isotope Labeling. In: Biophysical Journal. 2008, 94(2), pp. 610-613. ISSN 0006-3495. Available under: doi: 10.1016/S0006-3495(08)79104-5

BibTex

@article{Huang2008Trpzi-17611,
  year={2008},
  doi={10.1016/S0006-3495(08)79104-5},
  title={Trpzip-Based Beta-Hairpin Equilibrium and Temperature Jump IR Studies Enhanced by Site-Specific Isotope Labeling},
  number={2},
  volume={94},
  issn={0006-3495},
  journal={Biophysical Journal},
  pages={610--613},
  author={Huang, Rong and Krejtschi, Carsten and Hauser, Karin and Keiderling, Timothy A.}
}

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