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摘要
The fast folding/unfolding dynamics of the alpha-helical polypeptide poly-N-5-(3-hydroxypropyl)-L-glutamine, PHPG, was observed in D2O after a nanosecond laser-induced temperature jump of 1degreesC. The sudden rise in temperature disturbs the helix-coil equilibrium of the peptide and the ensuing structural relaxation was monitored by time-resolved IR-spectroscopy of the amide I' band with a time resolution of 12 ns. After an initial relaxation on the time scale of a few nanoseconds, probably arising from a local rearrangement of random coil or side chain structures, the helix-coil relaxation proceeds on the time scale of a few hundred nanoseconds. The observed time constant of 227 ns is very similar to the helix-coil relaxation time constants observed for short alanine-based peptides, in spite of the greater length and more complex and bulky side chain of PHPG.
- 出版日期2004
