Abstract
Photoswitches suitably connected to model peptides allow to apply light as trigger for folding initiation. Time-resolved infrared spectroscopy provides a certain degree of structural information and allows to follow the kinetics of photoinduced conformational changes by investigating the transient, interconverting structures. Several secondary structure elements have been studied in detail with this approach. The recent development of light-responsive tertiary structures yields the next generation of model peptides on the way toward an understanding of protein folding.
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Zinth, W., Wachtveitl, J. (2012). Light-Triggered Peptide Dynamics. In: Fabian, H., Naumann, D. (eds) Protein Folding and Misfolding. Biological and Medical Physics, Biomedical Engineering. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-22230-6_7
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