Publication Date:
2006-04-15
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mittermaier, Anthony -- Kay, Lewis E -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):224-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, McGill University, Montreal, Quebec H3A 2K6, Canada. anthony.mittermaier@mcgill.ca.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614210" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/chemistry
;
Chemistry, Physical
;
Kinetics
;
Motion
;
*Nuclear Magnetic Resonance, Biomolecular/methods
;
Physicochemical Phenomena
;
*Protein Conformation
;
*Protein Folding
;
Proteins/*chemistry
;
Proto-Oncogene Proteins c-fyn/chemistry
;
Temperature
;
Thermodynamics
;
src Homology Domains
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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