The use of proton‐enhanced, natural abundance <sup>13</sup>C NMR to study the molecular dynamics of model and biological membranes

Cornell, Bruce; Keniry, Max A.; Hiller, Roger G.; Smith, Ross

doi:10.1016/0014-5793(80)80743-5

Cited by 8 publications

(1 citation statement)

References 16 publications

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“…Cornell et a1 (1982) and Sefcik et al (1983) showed that the addition of p oteins or cholesterol to bilayer lipids was shown to produce low-frequency motions involving collective movements of large segments of hydrocarbon chain, as studied by T1 and ' & The present TYQ of the aliphatic portion of BL8SY is o f t ie same order of magnitude as that observed for a 1ipid-bila:'er system by Cornell et al (1982). Further, the correspondin) TCH is again very close to that observed for dimyristoylglyce ophosphocholine (Cornell et al, 1980). In view of the siriilarity of the dynamic behavior of the detergents and lipids, the detergent molecules in the crystals of membrane proteirs can be considered as boundary detergents which mimic bo indary lipids.…”

Section: Dynamic Aspects Of Protein and Detergent Interactionsupporting

confidence: 73%

A high‐resolution solid‐state ¹³C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme

Tuzi

Shinzawa‐Itoh

Erata

et al. 1992

European Journal of Biochemistry

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We have recorded 100.6-MHz high-resolution solid-state ' 3C-NMR spectra of crystalline cytochrome-c oxidase from bovine heart muscle and hen egg-white lysozyme, to compare conformation and dynamics of a typical membrane-protein complex with those of lysozyme. The absence of severe interference with the solid-state 13C-NMR spectra, from both the line broadenings from paramagnetic centers and overlapping of intense detergent signals, provided spectral resolution of 3C-NMR feature of cytochrome-c oxidase crystals comparable to that of lysozyme crystal and better than that of dissolved or lyophilized samples. In fact, the observed peak intensities of the polar heads of the detergents BL8SY and Brij 35 were only about 10% and 3% of the anticipated values, respectively.The dynamic behavior of the backbone and side chains of cytochrome-c oxidase was compared with that of lysozyme on the basis of the 13C spin-lattice relaxation times (Tl): the backbone of the cytochrome-c oxidase turned out to be more flexible than that of lysozyme. Molecular motions of the detergent molecules attached to the proteins are found to be highly heterogeneous. Detergent molecules undergo rapid tumbling motions in the crystals in about 10 ns as detected by T l . In addition to rapid motions, slow motions were detected by 'H spin-lattice relaxation time in the rotating frame ( TyQ) and cross-polarization time ( TCH), together with data from static spectra, indicating that the aliphatic portion of the detergent interacts more strongly with hydrophobic protein surfaces than do the polar heads.Knowledge of three-dimensional structure of atomic resolution is indispensable for understanding protein function. This goal will be, in principle, achieved by X-ray diffraction or multi-dimensional NMR spectroscopy combined with suitable molecular modelling (Wiithrich et al., 1986(Wiithrich et al., , 1989Clore and Gronenborn, 1991). This approach, however, is not always straightforward for transmembrane proteins, because crystallization of membrane proteins is extremely difficult compared with that of water-soluble proteins. Furthermore, many NMR peaks are masked by strong signals from the sohbilization detergent. In fact, only limited examples of three-dimensional structures of transmembrane proteins have been revealed by X-ray diffraction, such as the photosynthetic reaction center from Rhodopseudomonas viridis (Deisenhofer et al., 1985) and bacterial porin (Garavito and Rorsenbasch, 1980).

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Section: Dynamic Aspects Of Protein and Detergent Interactionsupporting

confidence: 73%

A high‐resolution solid‐state ¹³C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme

Tuzi

Shinzawa‐Itoh

Erata

et al. 1992

European Journal of Biochemistry

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Membranes: Carbon-13 NMR

Separovic

Cornell

2007

Encyclopedia of Magnetic Resonance

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NMR Studies of the Gel Phase of Lecithins and Cephalins

Trahms

1985

Structure and Dynamics of Molecular Systems

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The use of proton‐enhanced, natural abundance ¹³C NMR to study the molecular dynamics of model and biological membranes

Cited by 8 publications

References 16 publications

A high‐resolution solid‐state ¹³C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme

A high‐resolution solid‐state ¹³C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme

Membranes: Carbon-13 NMR

NMR Studies of the Gel Phase of Lecithins and Cephalins

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The use of proton‐enhanced, natural abundance 13C NMR to study the molecular dynamics of model and biological membranes

Cited by 8 publications

References 16 publications

A high‐resolution solid‐state 13C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme

A high‐resolution solid‐state 13C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme

Membranes: Carbon-13 NMR

NMR Studies of the Gel Phase of Lecithins and Cephalins

Contact Info

Product

Resources

About

The use of proton‐enhanced, natural abundance ¹³C NMR to study the molecular dynamics of model and biological membranes

A high‐resolution solid‐state ¹³C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme

A high‐resolution solid‐state ¹³C‐NMR study on crystalline bovine heart cytochrome‐c oxidase and lysozyme