The incorporation of fluorinated amino acids into proteins through natural biosynthesis in E. coli often leads to the production of heterogeneous fluorinated proteins. The stabilities of proteins with different ^(19)F labelling states can vary, but these differences are challenging to measure due to the difficulty in separating the fluorinated protein mixtures that differ by only a few ^(19)F atoms. Here, we simultaneously incorporated both fluoro-phenylalanines (3-fluoro-phenylalanine, 3FF; or...
Fluorine labelling for in situ 19F NMR in oriented systems
Fluorine labelling for in situ 19F NMR in oriented systems
Abstract
The focus of this project is to take advantage of the large NMR chemical shift anisotropy of 19F to determine the orientation of fluorine labeled biomolecules in situ in oriented biological systems such as muscle. The difficulty with a single fluorine atom is that the orientation determined from a chemical shift is not singlevalued in the case of a fully anisotropic chemical shift tensor. The utility of a labeling approach with two fluorine labels in a fixed molecular framework where...
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02-26-2024 09:15 PM
Simultaneous measurement of 1 H C/N -R 2 â?²s for rapid acquisition of backbone and sidechain paramagnetic relaxation enhancements (PREs) in proteins
Simultaneous measurement of 1 H C/N -R 2 â?²s for rapid acquisition of backbone and sidechain paramagnetic relaxation enhancements (PREs) in proteins
Abstract
Paramagnetic relaxation enhancements (PREs) are routinely used to provide long-range distance restraints for the determination of protein structures, to resolve protein dynamics, ligandâ??protein binding sites, and lowly populated species, using Nuclear Magnetic Resonance Spectroscopy (NMR). Here, we propose a simultaneous 1H-15Â*N, 1H-13C SESAME based pulse scheme for the rapid acquisition of...
Optimizing fluorine labelling for 19 F solid-state NMR in oriented biological systems
Optimizing fluorine labelling for 19 F solid-state NMR in oriented biological systems
Abstract
When planning a fluorine labeling strategy for 19F solid state NMR (ssNMR) studies of the structure and/or mobility of fluorine labeled compounds in situ in an oriented biological system, it is important to characterize the NMR properties of the label. This manuscript focuses on the characterization of a selection of aromatic fluorine compounds in dimyristoylphosphatidylcholine bilayers using 19F ssNMR from the standpoint of determiningÂ*the optimum...
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02-29-2020 09:52 PM
TROSY pulse sequence for simultaneous measurement of the 15 N R 1 and { 1 H}â?? 15 N NOE in deuterated proteins
TROSY pulse sequence for simultaneous measurement of the 15 N R 1 and { 1 H}â?? 15 N NOE in deuterated proteins
Abstract
A TROSY-based NMR experiment is described for simultaneous measurement of the 15N longitudinal relaxation rate constant R1 and the {1H}â??15N nuclear Overhauser enhancement. The experiment is based on the observation that the TROSY mixing pulse sequence element symmetrically exchanges 1H and 15N magnetizations. The accuracy of the proposed technique is validated by comparison to independent measurements of both relaxation parameters...
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04-16-2018 11:30 AM
[NMR paper] Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
Phys Chem Chem Phys. 2017 Jan 09;:
Authors: Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M
Abstract
RNA molecules in solution tend to undergo structural fluctuations of...
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01-12-2017 03:48 AM
Simultaneous Chirality Sensing of Multiple Amines by 19F NMR
Simultaneous Chirality Sensing of Multiple Amines by 19F NMR
Yanchuan Zhao and Timothy M. Swager
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b00556/20150227/images/medium/ja-2015-00556n_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b00556
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://www.bionmr.com//feeds.feedburner.com/~r/acs/jacsat/~4/EZ7QKbt4vFY
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02-27-2015 11:25 PM
Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins
Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins
Abstract A two-dimensional TROSY-based SIM-13Cmâ??1Hm/1Hâ??15N NMR experiment for simultaneous measurements of methyl 1 D CH and backbone amide 1 D NH residual dipolar couplings (RDC) in {U-; Ileδ1-; Leu,Val-}-labeled samples of large proteins is described. Significant variation in the alignment tensor of the 82-kDa enzyme Malate synthase G is observed as a function of only slight changes in experimental conditions. The SIM-13Cmâ??1Hm/1Hâ??15N data sets provide convenient means...
Simultaneous measurement of multiple fluorine labelling effect on GB1 stability by (19)F NMR
Linear Mode
