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  Speeding-up exchange-mediated saturation transfer experiments by Fourier transform.

Carneiro, M. G., Reddy, J. G., Griesinger, C., & Lee, D. (2015). Speeding-up exchange-mediated saturation transfer experiments by Fourier transform. Journal of Biomolecular NMR, 63(3), 237-244. doi:10.1007/s10858-015-9985-9.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-09BD-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-58FB-4
Genre: Journal Article

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 Creators:
Carneiro, M. G.1, Author              
Reddy, J. G., Author
Griesinger, C.1, Author              
Lee, D., Author
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1Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: CEST; Chemical exchange; DEST; Fourier transform; NMR; Protein dynamics
 Abstract: Protein motions over various time scales are crucial for protein function. NMR relaxation dispersion experiments play a key role in explaining these motions. However, the study of slow conformational changes with lowly populated states remained elusive. The recently developed exchange-mediated saturation transfer experiments allow the detection and characterization of such motions, but require extensive measurement time. Here we show that, by making use of Fourier transform, the total acquisition time required to measure an exchange-mediated saturation transfer profile can be reduced by twofold in case that one applies linear prediction. In addition, we demonstrate that the analytical solution for R1ρ experiments can be used for fitting the exchange-mediated saturation transfer profile. Furthermore, we show that simultaneous analysis of exchange-mediated saturation transfer profiles with two different radio-frequency field strengths is required for accurate and precise characterization of the exchange process and the exchanging states.

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Language(s): eng - English
 Dates: 2015-09-092015-11
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s10858-015-9985-9
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 63 (3) Sequence Number: - Start / End Page: 237 - 244 Identifier: -