Fluorine-19 Nuclear Magnetic Resonance Spectroscopy

Jones, Keith A.; Mooney, E.F.

doi:10.1016/s0066-4103(08)60385-3

Cited by 22 publications

(7 citation statements)

References 145 publications

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“…As a result, the principles of 19 F-NMR have been extensively described in the literature, including serial coverage in the Annual Reports on NMR Spectroscopy (starting with [1]) and monographs (for example, [2]). It was also readily recognized that the absence of a natural 19 F background and the high sensitivity of 19 F-NMR observation favor the use of fluorine-19 labels for studies of proteins.…”

Section: Introductionmentioning

confidence: 99%

Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs

Didenko

Liu

Horst

et al. 2013

Current Opinion in Structural Biology

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Fluorine-19 is a spin-½ NMR isotope with high sensitivity and large chemical shift dispersion, which makes it attractive for high resolution NMR spectroscopy in solution. For studies of membrane proteins it is further of interest that 19F is rarely found in biological materials, which enables observation of extrinsic 19F labels with minimal interference from background signals. Today, after a period with rather limited use of 19F-NMR in structural biology, we witness renewed interest in this technology for studies of complex supramolecular systems. Here we report on recent 19F-NMR studies with the G-protein-coupled receptor family of membrane proteins.

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Section: Introductionmentioning

confidence: 99%

Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs

Didenko

Liu

Horst

et al. 2013

Current Opinion in Structural Biology

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“…Several favorable nuclear spin properties of fluorine-19 ( 19 F), that have been exploited since the early days [6] are finding stronger footholds again. These include:…”

Section: Nuclear Magnetic Resonancementioning

confidence: 99%

“…TIRF (discussed below) and confocal microscopy are commonly employed in the detection of smFRET [94]. For time dependent analysis k ET = (R 0 /r) 6 (1/τ D ) (3) where τ D is the donor's fluorescence lifetime in the absence of the acceptor. FRET approaches have gained widespread popularity in recent years with the availability of fusion proteins such as green fluorescent protein (GFP) and/or its mutated derivatives.…”

mentioning

confidence: 99%

New Horizons in Structural Biology of Membrane Proteins: Experimental Evaluation of the Role of Conformational Dynamics and Intrinsic Flexibility

2022

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A plethora of membrane proteins are found along the cell surface and on the convoluted labyrinth of membranes surrounding organelles. Since the advent of various structural biology techniques, a sub-population of these proteins has become accessible to investigation at near-atomic resolutions. The predominant bona fide methods for structure solution, X-ray crystallography and cryo-EM, provide high resolution in three-dimensional space at the cost of neglecting protein motions through time. Though structures provide various rigid snapshots, only an amorphous mechanistic understanding can be inferred from interpolations between these different static states. In this review, we discuss various techniques that have been utilized in observing dynamic conformational intermediaries that remain elusive from rigid structures. More specifically we discuss the application of structural techniques such as NMR, cryo-EM and X-ray crystallography in studying protein dynamics along with complementation by conformational trapping by specific binders such as antibodies. We finally showcase the strength of various biophysical techniques including FRET, EPR and computational approaches using a multitude of succinct examples from GPCRs, transporters and ion channels.

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“…A number of summaries of fluorine NMR spectroscopy have appeared (Mooney and Winson, 1968;Jones and Mooney, 1970;Fields, 1972Fields, , 1977Barlow, 1971, 1974;Phillips, 1974;Cavalli, 1976) as well as compilations of reported fluorine chemical shifts (Dungan and Van Wazur, 1970;Emsley and Phillips, 1971). A useful discussion of experimental considerations in executing Fourier transform FMR experiments with fluorinecontaining biological systems has also appeared (Sykes and Hull, 1978).…”

Section: Fluorine Magnetic Resonance Experimentsmentioning

confidence: 99%

Biological Magnetic Resonance

1978

Biological Magnetic Resonance

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Fluorine-19 Nuclear Magnetic Resonance Spectroscopy

Cited by 22 publications

References 145 publications

Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs

Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs

New Horizons in Structural Biology of Membrane Proteins: Experimental Evaluation of the Role of Conformational Dynamics and Intrinsic Flexibility

Biological Magnetic Resonance

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