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  Recent advances in measuring the kinetics of biomolecules by NMR relaxation dispersion spectroscopy.

Ban, D., Smith, C. A., de Groot, B. L., Griesinger, C., & Lee, D. (2017). Recent advances in measuring the kinetics of biomolecules by NMR relaxation dispersion spectroscopy. Archives of Biochemistry and Biophysics, 628, 81-91. doi:10.1016/j.abb.2017.05.016.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-5D0B-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-08DF-C
Genre: Journal Article

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2451272.pdf (Publisher version), 3MB
 
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 Creators:
Ban, D., Author
Smith, C. A.1, Author              
de Groot, B. L.1, Author              
Griesinger, C.2, Author              
Lee, D.2, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: Protein dynamics; Nuclear magnetic resonance spectroscopy; Relaxation dispersion; Kinetics; Protein motion; Energy landscape
 Abstract: Protein function can be modulated or dictated by the amplitude and timescale of biomolecular motion, therefore it is imperative to study protein dynamics. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique capable of studying timescales of motion that range from those faster than molecular reorientation on the picosecond timescale to those that occur in real-time. Across this entire regime, NMR observables can report on the amplitude of atomic motion, and the kinetics of atomic motion can be ascertained with a wide variety of experimental techniques from real-time to milliseconds and several nanoseconds to picoseconds. Still a four orders of magnitude window between several nanoseconds and tens of microseconds has remained elusive. Here, we highlight new relaxation dispersion NMR techniques that serve to cover this "hidden-time" window up to hundreds of nanoseconds that achieve atomic resolution while studying the molecule under physiological conditions.

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Language(s): eng - English
 Dates: 2017-05-302017-08-15
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.abb.2017.05.016
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Title: Archives of Biochemistry and Biophysics
Source Genre: Journal
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Pages: - Volume / Issue: 628 Sequence Number: - Start / End Page: 81 - 91 Identifier: -