Limited chemical shift dispersion represents a significant barrier to studying multistate equilibria of large membrane proteins by ^(19)F NMR. We describe a novel monofluoroethyl ^(19)F probe that dramatically increases the chemical shift dispersion. The improved conformational sensitivity and line shape enable the detection of previously unresolved states in one-dimensional (1D) ^(19)F NMR spectra of a 134 kDa membrane transporter. Changes in the populations of these states in response to...
[ASAP] Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM
Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM
Yun Huang, Krishna D. Reddy, Clay Bracken, Biao Qiu, Wenhu Zhan, David Eliezer, and Olga Boudker
https://pubs.acs.org/cms/10.1021/jacs.3c01003/asset/images/medium/ja3c01003_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.3c01003
[ASAP] Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET
Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET
Gregory-Neal W. Gomes, Mickae?l Krzeminski, Ashley Namini, Erik W. Martin, Tanja Mittag, Teresa Head-Gordon, Julie D. Forman-Kay, and Claudiu C. Gradinaru
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c02088/20200904/images/medium/ja0c02088_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c02088
http://feeds.feedburner.com/~r/acs/jacsat/~4/ouvFj6sHuyQ
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[NMR paper] Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
Related Articles Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
J Am Chem Soc. 2020 Aug 25;:
Authors: Gomes GW, Krzeminski M, Namini A, Martin EW, Mittag T, Head-Gordon T, Forman-Kay JD, Gradinaru CC
Abstract
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which makes structural characterization challenging,...
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08-26-2020 02:46 PM
[NMR paper] Dual screening of BPTF and Brd4 using protein-observed fluorine NMR uncovers new bromodomain probe molecules.
Dual screening of BPTF and Brd4 using protein-observed fluorine NMR uncovers new bromodomain probe molecules.
Dual screening of BPTF and Brd4 using protein-observed fluorine NMR uncovers new bromodomain probe molecules.
ACS Chem Biol. 2015 Jul 9;
Authors: Urick AK, Hawk LM, Cassel MK, Mishra NK, Liu S, Adhikari N, Zhang W, Dos Santos CO, Hall JL, Pomerantz WC
Abstract
Bromodomain-containing protein dysregulation is linked to cancer, diabetes, and inflammation. Selec-tive inhibition of bromodomain function is a newly...
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07-12-2015 07:12 AM
[NMR paper] Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Proc Natl Acad Sci U S A. 2014 Oct 13;
Authors: Baxa MC, Haddadian EJ, Jumper JM, Freed KF, Sosnick TR
Abstract
The loss of conformational entropy is a major contribution in the thermodynamics of protein folding. However, accurate determination of the quantity...
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10-15-2014 10:58 AM
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
Abstract The combination of the wide availability of protein backbone and side-chain NMR chemical shifts with advances in understanding of their relationship to protein structure makes these parameters useful for the assessment of structural-dynamic protein models. A new chemical shift predictor (PPM) is introduced, which is solely based on physicalâ??chemical contributions to the chemical shifts for both the protein backbone and methyl-bearing amino-acid side chains. To...
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09-15-2012 09:04 AM
[NMR paper] Specific in vitro labeling of cells with a fluorine-19 probe encapsulated in antibody
Specific in vitro labeling of cells with a fluorine-19 probe encapsulated in antibody-targeted liposomes: a F-19 NMR spectroscopy study.
Related Articles Specific in vitro labeling of cells with a fluorine-19 probe encapsulated in antibody-targeted liposomes: a F-19 NMR spectroscopy study.
Magn Reson Med. 1993 Feb;29(2):252-5
Authors: Vion-Dury J, Machy P, Confort-Gouny S, Leserman L, Cozzone PJ
Liposomes containing dexamethasone phosphate (DMp) were covalently coupled to protein A and then incubated with murine L929 fibroblast and RDM4...
Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM
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