Protein mobility in membranes

Cherry, Richard J.

doi:10.1016/0014-5793(75)80943-4

Cited by 56 publications

(21 citation statements)

References 60 publications

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“…For Vpu, in contrast, signals from residues of both domains are affected to a much lesser degree by slow motions. As already demonstrated in 1975 (Cherry, 1975), membrane proteins in lipid bilayers may undergo fast rotational reorientation about the bilayer normal, which leads to a reduction of anisotropic interactions by a factor of 0.5 (3cos 2 ϕ-1), where ϕ is the tilt angle of the long axis of the TM helix toward the bilayer normal (Lewis et al, 1985). For the TM domain of Vpu, it could be demonstrated for various bilayer systems that the TM domain undergoes fast rotation about the bilayer normal, but not around the long axis of the helix (De Angelis et al, 2004;Park et al, 2006b).…”

Section: Cd4(372-433) Shows Higher Mobility In Popc Bilayers Than Fulsupporting

confidence: 65%

Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

Quynh¹,

Wittlich²,

Glück³

et al. 2013

Biological Chemistry

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HIV-1 Vpu and CD4(372-433), a peptide comprising the transmembrane and cytoplasmic domain of human CD4, were recombinantly expressed in Escherichia coli, uniformly labeled with 13 C and 15 N isotopes, and separately reconstituted into phospholipid bilayers. Highly resolved dipolar cross-polarization (CP)-based solid-state NMR spectra of the two transmembrane proteins were recorded under magic angle sample spinning. Partial assignment of 13 C resonances was achieved. Site-specific assignments were obtained for 13 amino acid residues of CD4(372-433) and two Vpu residues. Additional amino acid type-specific assignments were achieved for 10 amino acid spin systems for both CD4(372-433) and Vpu. Further, structural flexibility was probed with different dipolar recoupling techniques, and the correct insertion of the transmembrane domains into the lipid bilayers was confirmed by proton spin diffusion experiments.

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Section: Cd4(372-433) Shows Higher Mobility In Popc Bilayers Than Fulsupporting

confidence: 65%

Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

Quynh¹,

Wittlich²,

Glück³

et al. 2013

Biological Chemistry

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“…The translational mobility of membrane proteins and their redistribution after binding antibodies or lectins have recently attracted much attention (1)(2)(3)(4)(5)(6)(7)(8)(9). These phenomena have been discussed in terms of the fluid mosaic model (10) according to which membrane proteins are embedded in a fluid-like lipid bilayer, so that their translational and rotational diffusion are limited mainly by the viscosity of the lipid matrix (1,10).…”

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confidence: 99%

Lateral transport on cell membranes: mobility of concanavalin A receptors on myoblasts.

Schlessinger¹,

Koppel²,

Axelrod³

et al. 1976

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

256

144

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We report measurements of the lateral mobility of fluorescent labeled concanavalin A receptor complexes on the plasma membrane of cultured myoblasts of rat. Transport rates were measured by observing the recovery of fluorescence in a small region of the cell surface initially photobleached irreversibly by an intense, focused laser light pulse. Under different conditions we measured effective diffusion coefficients of the receptor complexes in the range 8 X 10-12 < D < 3 X 10-11 cm2/sec which is two orders of magnitude lower than we found for a fluorescent lipid probe, D (8 : We have directly measured the rate of lateral transport of fluorescent labeled concanavalin A (Con A) receptors on the plasma membrane of cultured myoblasts of rat. This paper presents a brief description of our methods and a preliminary account of our observations.The translational mobility of membrane proteins and their redistribution after binding antibodies or lectins have recently attracted much attention (1-9). These phenomena have been discussed in terms of the fluid mosaic model (10) according to which membrane proteins are embedded in a fluid-like lipid bilayer, so that their translational and rotational diffusion are limited mainly by the viscosity of the lipid matrix (1, 10). The first experimental demonstration of'lateral transport of membrane proteins was reported by Frye and Edidin (5). They measured the intermixing times of transplantation antigens after heterokaryon fusion and deduced an apparent diffusion constant of D -10-1°cm2/sec. A wide range of apparent diffusion coefficients of membrane proteins has been obtained in other systems: 1 to 2 X 10-9 cm2/sec for transplantation antigens on a muscle fiber (7), 4 to 5 X 10-9 cm2/sec for rhodopsin in amphibian discs (8), and <3 X 10-12 cm2/sec for nonspecifically labeled proteins in erythrocyte membranes (9). The patching (11) and capping (2, 12) of antibodies and lectins on cell surfaces are visible manifestations of protein mobility in cell membranes. Metabolic inhibitors prevent capping (12) but not patching (11). Moreover, colchicine and colcemid, inhibitors of microtubule assembly (13,14), affect capping in lymphoAbbreviations: Hanks' BSS, Hanks' balanced salt solution; Con A, concanavalin A; S-Con A, succinyl concanavalin A; FITC, fluorescein isothiocyanate; FPR, fluorescence photobleaching recovery; FCS, fluorescence correlation spectroscopy; diI, 3,3'-dioctadecylindocarbocyanine iodide; a-MeMan, methyl a-D-mannopyranoside. 2409 cytes, and suggests that these internal structures are somehow involved in the translational mobility of some membrane components (15,16).It is therefore of great interest to directly observe the rate of lateral transport of membrane proteins and lipids in order to test the fluid mosaic model. We have chosen Con A for our first investigation of lateral transport in membranes because its effects on lateral and rotational mobility have been invoked to explain or characterize a number of interesting cellular phenomena (3,(17)(18)(19).We ha...

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“…The rotational diffusion of membrane proteins in phospholipid bilayers, illustrated in Figure 10, was shown to occur in the early 1970s by optical methods [15–19, 84, 90]. Notably, the same phenomenon was observed in the averaging of lineshapes by NMR.…”

Section: Rotationally Aligned Solid-state Nmrmentioning

confidence: 78%

“…This is illustrated in Figure 10 by the representation of Singer and Nicholson’s fluid mosaic model of a biological membrane [101]. Both the phospholipids and the proteins undergo fast rotational diffusion about the bilayer normal [15, 21], as indicated by the arrows, as well as translational diffusion in the plane of the bilayer.…”

Section: Rotationally Aligned Solid-state Nmrmentioning

confidence: 99%

The development of solid-state NMR of membrane proteins

Opella

2014

Biomedical Spectroscopy and Imaging

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Protein mobility in membranes

Cited by 56 publications

References 60 publications

Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

Lateral transport on cell membranes: mobility of concanavalin A receptors on myoblasts.

The development of solid-state NMR of membrane proteins

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