New Tools Provide New Insights in NMR Studies of Protein Dynamics

There is growing evidence that structural flexibility plays a central role in the function of protein molecules. Many of the experimental data come from nuclear magnetic resonance (NMR) spectroscopy, a technique that allows internal motions to be probed with exquisite time and spatial resolution. Re...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2006-04, Vol.312 (5771), p.224-228
Main Authors: Mittermaier, Anthony, Kay, Lewis E
Format: Article
Language:English
Subjects:
Amides
Bacterial Proteins - chemistry
Biochemistry
Chemical equilibrium
Chemical Phenomena
Chemistry, Physical
Geometric lines
Kinetics
Lead
Magnetic fields
Molecules
Motion
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Conformation
Protein Folding
Proteins
Proteins - chemistry
Proto-Oncogene Proteins c-fyn - chemistry
Reviews
Spectral resolution
Spectroscopy
src Homology Domains
Temperature
Thermodynamics
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Summary:There is growing evidence that structural flexibility plays a central role in the function of protein molecules. Many of the experimental data come from nuclear magnetic resonance (NMR) spectroscopy, a technique that allows internal motions to be probed with exquisite time and spatial resolution. Recent methodological advancements in NMR have extended our ability to characterize protein dynamics and promise to shed new light on the mechanisms by which these molecules function. Here, we present a brief overview of some of the new methods, together with applications that illustrate the level of detail at which protein motions can now be observed.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1124964