Abstract
When a protein finds its native three-dimensional structure from the unstructured amino-acid chain various processes over a large time range are relevant. To understand the pathway of protein folding, and in particular the physico-chemical mechanism, one needs to cover the entire folding/refolding reaction (U ↔ N) on a structural level. Especially processes in the ns to ms time range seem to be fundamental for unfolding
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© 1997 Springer Science+Business Media Dordrecht
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Georg, H., Siebert, F. (1997). Temperature Induced Protein Unfolding and Refolding Studied by Time-Resolved Infrared Spectroscopy. In: Carmona, P., Navarro, R., Hernanz, A. (eds) Spectroscopy of Biological Molecules: Modern Trends. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5622-6_2
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DOI: https://doi.org/10.1007/978-94-011-5622-6_2
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6369-2
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