Abstract
For most proteins the primary sequence encodes the native structure as well as the dynamics of the folding process. Recent theoretical models propose complex energy landscapes, which efficiently funnel the folding towards the native form(s) [1–4]. It is essential to develop methods to predict the structure of functioning and mutated proteins from their primary sequences in order to devise strategies for alleviating human disease. We report here the first nsec transient UV resonance Raman spectroscopy (UVRS) to investigate the earliest events in protein structural evolution. We examined the thermal unfolding of the α-helical peptide A5[AAARA]3A (AP).
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© 1999 Springer Science+Business Media Dordrecht
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Lednev, I.K., Karnoup, A.S., Sparrow, M.C., Asher, S.A. (1999). Nanosecond UV resonance Raman examination of initial steps in α-helix secondary structure evolution. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_3
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DOI: https://doi.org/10.1007/978-94-011-4479-7_3
Publisher Name: Springer, Dordrecht
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