Protein dynamics: From molecules, to interactions, to biology

Research output: Contribution to journalReview article

Abstract

Proteins have a remarkably rich diversity of dynamical behaviors, and the articles in this issue of the International Journal of Molecular Sciences are a testament to that fact. From the picosecond motions of single sidechains probed by NMR or fluorescence spectroscopy, to aggregation processes at interfaces that take months, all time scales play a role. Proteins are functional molecules, so by their nature they always interact with their environment. This environment includes water, other biomolecules, or larger cellular structures. In a sense, it also includes the protein molecule itself: proteins are large enough to fold and interact with themselves. These interactions have been honed by evolution to produce behaviors completely different from those of random polymers.

Original languageEnglish (US)
Pages (from-to)1360-1368
Number of pages9
JournalInternational journal of molecular sciences
Volume10
Issue number3
DOIs
StatePublished - Mar 1 2009

Fingerprint

biology
proteins
Proteins
Molecules
molecules
interactions
Fluorescence Spectrometry
Fluorescence spectroscopy
Biomolecules
Cellular Structures
Nuclear magnetic resonance spectroscopy
Polymers
Magnetic Resonance Spectroscopy
Agglomeration
fluorescence
nuclear magnetic resonance
Water
polymers
water
spectroscopy

Keywords

  • Downhill folding
  • Evolution
  • Protein function

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

Cite this

Protein dynamics : From molecules, to interactions, to biology. / Gruebele, Martin.

In: International journal of molecular sciences, Vol. 10, No. 3, 01.03.2009, p. 1360-1368.

Research output: Contribution to journalReview article

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