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CPMG Experiments for Protein Minor Conformer Structure Determination

Gopalan, AB; Hansen, DF; Vallurupalli, P; (2018) CPMG Experiments for Protein Minor Conformer Structure Determination. Methods in Molecular Biology , 1688 pp. 223-242. 10.1007/978-1-4939-7386-6_11. Green open access

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Abstract

CPMG relaxation dispersion NMR experiments have emerged as a powerful method to characterize protein minor states that are in exchange with a visible dominant conformation, and have lifetimes between ~0.5 and 5 milliseconds (ms) and populations greater than 0.5%. The structure of the minor state can, in favorable cases, be determined from the parameters provided by the CPMG relaxation dispersion experiments. Here, we go through the intricacies of setting up these powerful CPMG experiments.

Type: Article
Title: CPMG Experiments for Protein Minor Conformer Structure Determination
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1007/978-1-4939-7386-6_11
Publisher version: http://dx.doi.org/10.1007/978-1-4939-7386-6_11
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: CPMG, Conformational dynamics, NMR, Protein, Relaxation dispersion
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/10042929
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