Protein Folding and Misfolding pp 147-170 | Cite as
Dynamics of α-Helix and β-Sheet Formation Studied by Laser-Induced Temperature-Jump IR Spectroscopy
Abstract
Analysis of folding mechanisms requires a fast initiation method besides site-specific structural probes. Laser-induced temperature-jump IR spectroscopy is an ideally suited method to study α-helix and β-sheet formation in the nanosecond-to-microsecond time domain. The section gives an overview about the T-jump technique and its power to obtain site-specific dynamics by a combination with isotopic editing.
Keywords
Probe Beam Temperature Jump Stokes Line Folding Mechanism Heated VolumeNotes
Acknowledgements
The author thanks Dr. Carsten Krejtschi, former PhD student for the initial work on the spectrometer setup and various T-jump studies and Timothy A. Keiderling, University of Illinois at Chicago (USA), for inspiring collaboration and for generously providing us with isotopically labeled peptide variants.
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