Dynamic fluctuation of proteins watched in real time

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The dynamic nature of protein function is a fundamental concept in the physics of proteins. Although the basic general ideas are well accepted most experimental evidence has an indirect nature. The detailed characterization of the dynamics is necessary for the understanding in detail. The dynamic fluctuations thought crucial for the function span an extremely broad time, starting from the picosecond regime. Recently, a few new experimental techniques emerged that permit the observation of dynamical phenomena directly. Notably, pulsed infrared (IR) spectroscopy has been applied with great success to observe structural changes with picosecond time resolution. Using two-dimensional-IR vibrational echo chemical exchange spectroscopy Ishikawa and co-workers [Ishikawa et al. (2008), Proc. Natl. Acad. Sci. U.S.A. 101, 14402-14407] managed to observe the transition between well defined conformational substrates of carbonmonoxy myoglobin directly. This is an important step in improving our insight into the details of protein function.

Original languageEnglish
Pages (from-to)297-301
Number of pages5
JournalHFSP Journal
Volume2
Issue number6
DOIs
Publication statusPublished - Dec 2008

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Spectrum Analysis
Proteins
Myoglobin
Physics
Infrared spectroscopy
Observation
Spectroscopy
Infrared radiation
Substrates

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Neuroscience(all)

Cite this

Dynamic fluctuation of proteins watched in real time. / Ormos, P.

In: HFSP Journal, Vol. 2, No. 6, 12.2008, p. 297-301.

Research output: Contribution to journalArticle

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