Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy
Article Abstract:
Theoretical and experimental advances have made [R.sub 1p.] measurement much more powerful for characterizing microsecond to millisecond conformational dynamics and chemical kinetics in proteins and other biomacromolecules. Chemical exchange is a ubiquitous phenomenon in NMR spectroscopy that mediates population transfer among longitudinal spin operators, affects line shapes in free-procession NMR spectra and its interest contributes to relaxation of magnet.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2006
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Fast-Time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
Article Abstract:
For the past 15 years there has been an explosion of research on the dynamical properties of proteins, largely driven by the emergence of a handful of techniques that are sensitive to protein motion with one method, nuclear magnetic relaxation (NMR) being applied in hundreds of protein. The NMR studies have indicated which aspect of dynamics is conserved or variant through a protein structure or between different proteins.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2006
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Molecular dynamics: Survey of methods for stimulating the activity of proteins
Article Abstract:
An outline is presented of the origin of molecular dynamics simulation for protein systems and how it has developed into a robust and trusted tool. Molecular dynamics simulations, along with a range of complementary computational approaches have become a valuable tool for investigating the basis of protein structure and function.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2006
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