Shakspeariana

Henderson, W. A.

doi:10.1093/nq/s8-vi.138.123b

Cited by 36 publications

(47 citation statements)

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“…The corrected spectra yield quantitative estimates of protein secondary structure [14]. The [19] at 222 nm, which can be taken as a rough index of the amount of a-helical structure [ 15 1, is about 10% less at pH 3 .O than at pH 6.0.…”

Section: Resultsmentioning

confidence: 99%

The low pH species of bacteriorhodopsin

Tsuji

Rosenheck

1979

FEBS Letters

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Section: Resultsmentioning

confidence: 99%

The low pH species of bacteriorhodopsin

Tsuji

Rosenheck

1979

FEBS Letters

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“…Interestingly, the charge density matching between anionically charged PR extramembrane domains and the cationic membranes still drives the spontaneously assembly of PR molecules into cationic lipid bilayers, and highly ordered PR 2D crystals form (peaks marked by blue arrows). The scatterings are at 0.072, 0.125, 0.144, 0.190, 0.216, 0.259, 0.288, and 0.314 Å Ϫ1 , corresponding to q 10 , q 11 , q 20 , q 21 , q 30 , q 31 , q 40 , and q 32 correlations of a PR 2D hexagonal lattice, respectively. The strong PR correlations suggest coherent orientation analogous to bR in purple membrane patches (40).…”

Section: Cl-pr Lamellar Superlattice Structures With Controlled Pr 3dmentioning

confidence: 99%

The directed cooperative assembly of proteorhodopsin into 2D and 3D polarized arrays

Liang

Whited²,

Nguyen

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Proteorhodopsin is the membrane protein used by marine bacterioplankton as a light-driven proton pump. Here, we describe a rapid cooperative assembly process directed by universal electrostatic interactions that spontaneously organizes proteorhodopsin molecules into ordered arrays with well defined orientation and packing density. We demonstrate the charge density-matching mechanism that selectively controls the assembly process. The interactions among different components in the system are tuned by varying their charge densities to yield different organized transmembrane protein arrays: (i) a bacteriorhodopsin purple membrane-like structure where proteorhodopsin molecules are cooperatively arranged with charged lipids into a 2D hexagonal lattice; (ii) selected liquid-crystalline states in which crystalline lamellae made up of the coassembled proteorhodopsin and charged lipid molecules are coupled three-dimensionally with polarized proteorhodopsin orientation persisting through the macroscopic scale. Understanding this rapid electrostatically driven assembly process sheds light on organizing membrane proteins in general, which is a prerequisite for membrane protein structural and mechanistic studies as well as in vitro applications.cationic lipid-proteorhodopsin complexes ͉ membrane protein arrays ͉ membrane protein crystallization ͉ light-driven proton pump ͉ photovoltaics M embrane proteins (MPs) play an essential role in determining the interactions of biological systems with their surroundings. As gatekeepers of cellular boundaries, they are involved with matter, energy, and information transport to maintain life activities, and also with drug delivery to cure diseases. MPs are estimated to represent 20-30% of the currently sequenced genomes (1), and are targets for Ϸ70% of all drugs in the market (2). Although the sequence and function of many MPs have become known, their structures have only been solved at a rate of Ϸ0.2% of that of soluble proteins (3). Little is known about how to harness their unique biological functions in practical devices.Long-range ordering is the prerequisite for structure determination, and unidirectional packing is needed for many in vitro applications depending on MP orientation because the activities of most MPs have vectorial aspects (4). The key problem that hinders MP assembly is their amphiphilic character. Except for a very limited number of MPs that form ordered crystals naturally, most MPs require detergents to free them from their native membranes. Although detergent-solubilized MPs with the surrounding detergent micelle in place could be crystallized (5), the orientation of MPs in those crystals is more or less isotropic, and the effect of lacking the biological membrane confinement on MP structure and mechanistic properties is always a concern. Detergent-assisted reconstitution is the most commonly used strategy to form 2D proteolipsome arrays (6). The MP order in those arrays depends critically on the detergent removal kinetics. Moreover, the lipid versus protein rat...

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“…The monomer is composed of seven rod-like structures. The rods were found to be c~-helices by X-ray diffraction (Henderson, 1975;Blaurock, 1975), and are approximately parallel to each other and parallel to the z axis. Circular symmetrical intensity functions were calculated for the monomer and trimer by the formula given by Oster & Riley (1952).…”

Section: Estimation Of Ao(u) For Arrangements Of Baeteriorhodopsimentioning

confidence: 99%

“…Fig. 2 shows intensity functions for the monomer and trimer of bacteriorhodopsin molecules, and the intensity for purple membrane which was taken from Henderson (1975). two-dimensional hexagonal lattice with a = 62.7 A, the structure of the purple membrane is formed.…”

Section: Estimation Of Ao(u) For Arrangements Of Baeteriorhodopsimentioning

confidence: 99%

The significance of the radial autocorrelation function for the interpretation of equatorial diffraction from biological membranes

Kataoka¹,

Ueki²

1980

Acta Cryst Sect A

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Oriented specimens of biomembranes give distinct Xray diffraction patterns of circular symmetry along the equatorial plane. In order to interpret such a diffraction pattern, properties of the radial autocorrelation function were examined in detail in conjunction with electron-density distribution and applied. The radial autocorrelation function, which is the Fourier-Bessel transform of an intensity function with circular symmetry, is the radial projection of a twodimensional autocorrelation function and can be interpreted in terms of Fourier components of electrondensity projection along the membrane normal. Some useful information is obtainable on the structure of the scatterer: (i) the approximate size of the X-ray scatterer; (ii)judgement of crystalline or non-crystalline arrangement of molecules; (iii) the existence of a regular arrangement of the electron-density fluctuations in a projection along the membrane normal; (iv) the rotational symmetry element existing in the scatterer if any.

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Shakspeariana

Cited by 36 publications

References 0 publications

The low pH species of bacteriorhodopsin

The low pH species of bacteriorhodopsin

The directed cooperative assembly of proteorhodopsin into 2D and 3D polarized arrays

The significance of the radial autocorrelation function for the interpretation of equatorial diffraction from biological membranes

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