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α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy
Open accessAbstract
Photo-triggered α-helix formation of a 16-residue peptide featuring a built-in conformational photoswitch is monitored by time-resolved IR spectroscopy. An experimental approach with 2-ps time resolution and a scanning range up to 30 μs is used to cover all time scales of the peptide dynamics. Experiments are carried out at different temperatures between 281 and 322 K. We observe single-exponential kinetics of the amide I′ band at 322 K on a time scale comparable to a recent temperature-jump folding experiment. When lowering the temperature, the kinetics become slower and nonexponential. The transition is strongly activated. Spectrally dispersed IR measurements provide multiple spectroscopic probes simultaneously in one experiment by resolving the amide I′ band, isotope-labeled amino acid residues, and side chains. We find differing relaxation dynamics at different spectral positions.
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Cites
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Cited by
Infrared Difference Spectroscopy of Proteins: From Bands to Bonds
Lorenz-Fonfria, V. A. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00449 · Cited by 325
Ali, A. M., Forbes, M. W., & Woolley, G. A. (2015) · ChemBioChem · doi:10.1002/cbic.201500191 · Cited by 25
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Metadata
- Authors
- Bredenbeck, J., Helbing, J., Kumita, J. R., Woolley, G. A., & Hamm, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-02-07
- Volume
- 102
- Issue
- 7
- Pages
- 2379-2384
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2028909116
- Cited by
- 189
- References
- 1
- FWCI
- 7.14
- Type
- journal article
- Language
- en
- Open access
- green
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- Bredenbeck, J., Helbing, J., Kumita, J. R., Woolley, G. A., & Hamm, P. (2005). α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0406948102
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