A fluorine NMR study of model membranes containing <sup>19</sup>F‐labeled phospholipids and an intrinsic membrane protein

Post, Jan F. M.; Ruiter, E.E.J.De; Berendsen, H.J.C.

doi:10.1016/0014-5793(81)81173-8

Cited by 15 publications

(8 citation statements)

References 23 publications

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“…However, it can also be applied to acquire homonuclear dipolar spectra from static samples and measure distances and/or angles between 19 F-spins [33,60,62,72,73]. While the train of 1808-pulses keeps refocusing the CSA and all heteronuclear couplings, the 19 F homonuclear interaction remains unaffected and continues to evolve during the echo intervals ( Fig.…”

Section: Cpmg Pulse Trainsmentioning

confidence: 98%

Solid state 19F NMR methods for studying biomembranes

Ulrich

2005

Progress in Nuclear Magnetic Resonance Spectroscopy

146

108

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Section: Cpmg Pulse Trainsmentioning

confidence: 98%

Solid state 19F NMR methods for studying biomembranes

Ulrich

2005

Progress in Nuclear Magnetic Resonance Spectroscopy

146

108

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“…Alternatively, r and can also be determined from a single oriented sample by varying its align- ment in the external magnetic field (42). The technique used in this study to measure the dipolar coupling is based on the CPMG sequence (32,33), which has already been successfully applied to determine internuclear distances and to evaluate motionally averaged order parameters (23,24,26,34,35). Oriented samples of fluorinated lipid bilayers have also been used previously for solid-state NMR investigations (25).…”

Section: Combination Of Distance and Orientation Measurementsmentioning

confidence: 99%

“…Many fluorinated proteins have been investigated in terms of their structure and function, and in most cases the perturbation of the system was negligible (10 -13 (17,18), and heteronuclear couplings from 19 F to 31 P, 13 C, or 15 N have been used for structural studies on various polymers and biological systems (19 -22). Many years back, Post et al determined segmental order parameters from the homonuclear dipolar coupling between geminal 19 F-labels on acyl chains in liquid crystals and membranes (8,(23)(24)(25)(26). In each case it was necessary to isolate the desired dipolar interaction from all other interactions, such that the coupling strength could be interpreted in terms of internuclear distance or orientation.…”

Section: Introductionmentioning

confidence: 98%

Structural Parameters from19F Homonuclear Dipolar Couplings, Obtained by Multipulse Solid-State NMR on Static and Oriented Systems

Grage

Ulrich

1999

Journal of Magnetic Resonance

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“…The effects of cholesterol and a membrane protein on 19Flabeled dimyristoylphosphatidylcholine (DMPC) were also studied by using the CPMG sequence (Post et al, 1981).…”

mentioning

confidence: 99%

Fluorine-19 nuclear magnetic resonance investigation of fluorine-19-labeled phospholipids. 1. A multiple-pulse study

Post¹,

Cook²,

Dowd³

et al. 1984

Biochemistry

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A multiple-pulse nuclear magnetic resonance technique has been used to measure the order parameter, SFF, at 40 MHz for dimyristoylphosphatidylcholine labeled with a difluoromethylene group at the 4-, 8-, or 12-position of the sn-2-acyl chain dispersed in water in the liquid-crystalline phase. The Carr-Purcell-Meiboom-Gill multiple-pulse sequence can resolve the homonuclear dipolar coupling between the two fluorine nuclei, thus making a direct determination of the order parameter, SFF, for the F-F internuclear vector possible. Other interactions, such as the 19F chemical shift anisotropy, heteronuclear dipolar couplings, and field inhomogeneity, which normally obscure the dipolar splitting, are effectively canceled. The order parameters obtained in this work compare well with those obtained by 19F nuclear magnetic resonance line-shape analysis of the 19F-labeled phospholipids reported in the following paper [Dowd, S. R., Simplaceanu, V., & Ho, C. (1984) Biochemistry (following paper in this issue)] as well as comparable SCD order parameters, determined for the deuterium-carbon internuclear vector of deuterium-labeled phospholipids [Oldfield, E., Meadows, M., Rice, D., & Jacobs, R. (1978) Biochemistry 17, 2727-2740]. The present results clearly show the usefulness of using nuclear magnetic resonance spectroscopy to investigate lipid-lipid and protein-lipid interactions, especially for those systems containing a difluoromethylene group in the acyl chain of a phospholipid molecule.

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A fluorine NMR study of model membranes containing ¹⁹F‐labeled phospholipids and an intrinsic membrane protein

Cited by 15 publications

References 23 publications

Solid state 19F NMR methods for studying biomembranes

Solid state 19F NMR methods for studying biomembranes

Structural Parameters from19F Homonuclear Dipolar Couplings, Obtained by Multipulse Solid-State NMR on Static and Oriented Systems

Fluorine-19 nuclear magnetic resonance investigation of fluorine-19-labeled phospholipids. 1. A multiple-pulse study

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A fluorine NMR study of model membranes containing 19F‐labeled phospholipids and an intrinsic membrane protein

Cited by 15 publications

References 23 publications

Solid state 19F NMR methods for studying biomembranes

Solid state 19F NMR methods for studying biomembranes

Structural Parameters from19F Homonuclear Dipolar Couplings, Obtained by Multipulse Solid-State NMR on Static and Oriented Systems

Fluorine-19 nuclear magnetic resonance investigation of fluorine-19-labeled phospholipids. 1. A multiple-pulse study

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A fluorine NMR study of model membranes containing ¹⁹F‐labeled phospholipids and an intrinsic membrane protein