Fast Events in Protein Folding: The Time Evolution of Primary Processes

Robert H. Callender, R. Brian Dyer, Rudolf Gilmanshin, William H. Woodruff

Research output: Contribution to journalArticle

181 Scopus citations

Abstract

Most experimental studies on the dynamics of protein folding have been confined to timescales of 1 ms and longer. Yet it is obvious that many phenomena that are obligatory elements of the folding process occur on much faster timescales. For example, it is also now clear that the formation of secondary and tertiary structures can occur on nanosecond and microsecond times, respectively. Although fast events are essential to, and sometimes dominate, the overall folding process, with a few exceptions their experimental study has become possible only recently with the development of appropriate techniques. This review discusses new approaches that are capable of initiating and monitoring the fast events in protein folding with temporal resolution down to picoseconds. The first important results from those techniques, which have been obtained for the folding of some globular proteins and polypeptide models, are also discussed.

Original languageEnglish (US)
Pages (from-to)173-202
Number of pages30
JournalAnnual Review of Physical Chemistry
Volume49
Issue number1
DOIs
StatePublished - Jan 1 1998

Keywords

  • Denaturation
  • Early folding intermediates
  • Infrared spectroscopy
  • Kinetics
  • Temperature jump

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Fingerprint Dive into the research topics of 'Fast Events in Protein Folding: The Time Evolution of Primary Processes'. Together they form a unique fingerprint.

  • Cite this