Alpha-helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy.

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.

authors

Bredenbeck J,Helbing J,Kumita JR,Woolley GA,Hamm P

doi

10.1073/pnas.0406948102

keywords:

subject

Has Abstract

pub_date

2005-02-15 00:00:00

pages

2379-84

issue

7

eissn

0027-8424

issn

1091-6490

pii

0406948102

journal_volume

102

pub_type

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