Abstract:
:Photo-triggered alpha-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 micros 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.
journal_name
Proc Natl Acad Sci U S Aauthors
Bredenbeck J,Helbing J,Kumita JR,Woolley GA,Hamm Pdoi
10.1073/pnas.0406948102keywords:
subject
Has Abstractpub_date
2005-02-15 00:00:00pages
2379-84issue
7eissn
0027-8424issn
1091-6490pii
0406948102journal_volume
102pub_type
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