Primary peptide folding dynamics observed with ultrafast temperature jump

Omar F. Mohammed, Gouri S. Jas, Milo M. Lin, Ahmed H. Zewail

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

Fastest folding: An ultrafast laser temperature jump (T-jump) induces folding and unfolding of Wh5 (see picture), the shortest possible α-helical peptide. Using time-resolved fluorescence spectroscopy, the folding time of this peptide was found to span from less than one nanosecond to a few nanoseconds, redefining the meaning of ultrafast dynamics in protein and peptide folding.

Original languageEnglish (US)
Pages (from-to)5628-5632
Number of pages5
JournalAngewandte Chemie - International Edition
Volume48
Issue number31
DOIs
StatePublished - Jul 20 2009
Externally publishedYes

Keywords

  • Helix-coil transitions
  • Peptide folding
  • Protein dynamics
  • Time-resolved spectroscopy

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

Fingerprint

Dive into the research topics of 'Primary peptide folding dynamics observed with ultrafast temperature jump'. Together they form a unique fingerprint.

Cite this