Protein rotational diffusion and lipid structure of reconstituted systems of Ca2+-activated adenosine triphosphatase

Hoffmann, Winfried; Sarzala, M.G.; Gómez‐Fernández, Juan C.; Goñi, Félix M.; Restall, Colin J.; Chapman, D.; Heppeler, G.; Kreutz, W.

doi:10.1016/0022-2836(80)90380-0

Cited by 44 publications

(15 citation statements)

References 19 publications

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“…9 8 and 9C we see that the transition Fig. 108, while the measurements reported by Hoffmann et al (63) are shown in Fig. 18B.…”

Section: Computer Simulation Of a Model Of A Pc Bilayer Containing Inmentioning

confidence: 60%

“…18B. It can be seen that the agreement is good, but that the calculations predict that the dependence is not linear as drawn by Hoffmann et al (63) but a curve reflecting the shape of the upper phase boundary. Finally, the general shape of the phase diagram predicted by our model is similar to that recently reported by Davis (Fig.…”

Section: Computer Simulation Of a Model Of A Pc Bilayer Containing Inmentioning

confidence: 62%

“…), decreases m s n o t o n i a y as x increases. When T = 40°C the dependence of (r2), upon x becomes more (63). Their data have been replotted here.…”

Section: Computer Simulation Of a Model Of A Pc Bilayer Containing Inmentioning

confidence: 93%

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Theoretical studies of phospholipid bilayers and monolayers. Perturbing probes, monolayer phase transitions, and computer simulations of lipid–protein bilayers

Pink¹

1984

Can. J. Biochem. Cell Biol.

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This paper describes some mathematical models for studying properties of lipid bilayer membranes. It is shown that there is evidence from fluorescent probe and electron spin resonance studies that some integral proteins are "randomly" distributed in the plane of a lipid bilayer for T greater than Tc, so that protein-protein "contacts" can occur. This implies that there is no permanent annulus of lipids around these proteins, so that there is no unique stoichiometric ratio of "boundary lipids" to protein. Computer simulation techniques are reviewed and comments are made about some recently introduced methods. Dynamical models of lipid--integral protein bilayers are outlined and it is shown that much differential scanning calorimetry, freeze-fracture, X-ray, and 2H nuclear magnetic resonance data can be understood. It is predicted that specific heat curves should show a rise at a temperature, TK less than Tc, at which a protein-rich phase starts to "melt"; that dipalmitoyl phosphatidylcholine (DPPC) hydrocarbon chains in such a protein-rich phase should exhibit some static disorder down to approximately -10 degrees C, around which they should freeze noncooperatively; and that the crossing of phase boundaries, as protein concentration expressed as mole fraction X changes just below Tc, should be reflected in a complicated dependence of protein lateral motion upon X. Models to study the liquid condensed-liquid expanded (LC-LE) transition of phosphatidylcholine (PC) monolayers at the air-water interface are described. The rounding in the LC phase of pressure-area isotherms are understood as the melting of microscopic gel-phase "domains" into macroscopic regions of fluid-phase lipids. There is some experimental support for this. Finally, to model the difference between a monolayer and the corresponding bilayer, an interaction is introduced between the two halves of a bilayer. It is shown to be very weak in the case of PC bilayers and it is outlined in the paper how monolayer and bilayer thermodynamics can be related. It was found that the internal lateral pressure of a DPPC bilayer is approximately 30 dyn/cm (1 dyn = 10 microN).

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“…9 8 and 9C we see that the transition Fig. 108, while the measurements reported by Hoffmann et al (63) are shown in Fig. 18B.…”

Section: Computer Simulation Of a Model Of A Pc Bilayer Containing Inmentioning

confidence: 60%

Section: Computer Simulation Of a Model Of A Pc Bilayer Containing Inmentioning

confidence: 62%

See 1 more Smart Citation

Theoretical studies of phospholipid bilayers and monolayers. Perturbing probes, monolayer phase transitions, and computer simulations of lipid–protein bilayers

Pink¹

1984

Can. J. Biochem. Cell Biol.

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“…Some authors even proposed that proteins would be surrounded at all times by a long-lived "annulus" of lipids that would, among other things, prevent protein-protein contacts. This view was challenged at that time by Chapman and co-workers Hoffmann et al, 1980) who provided evidence that, for integral membrane proteins reconstituted in pure phospholipids, when the lipid was in the fluid state proteins and lipids were diffusing at random in the plane of the bilayer, with only occasional transient contacts between protein molecules. However, when the system was cooled down below the phospholipid phase transition temperature, so that the lipid acyl chains became rigid and ordered (in the gel state), then lateral phase separation occurred, with formation of pure lipid domains distinct from those containing mainly protein.…”

Section: Ceramide-induced Protein-protein Contactsmentioning

confidence: 98%

Compartmentalization of ceramide signaling: physical foundations and biological effects

2000

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“…Other studies, both in our own laboratory (Hoffmann et al, 1979(Hoffmann et al, , 1980Restall et al, 1981) and elsewhere Thomas & Hidalgo, 1978;Burkli & Cherry, 1981;Thomas et al, 1982;Speirs et al, 1983), have shown that the (Ca'+-Mg'+)ATPase from sarcoplasmic reticulum exhibits rotational movement on the micro-to millisecond time scale both in its natural membrane and in fluid-reconstituted systems. Furthermore, the evidence suggests that an environmental condition that allows this movement, or possibly rotational freedom per se, is necessary for the biological activity of the protein.…”

mentioning

confidence: 93%

Rotational diffusion of calcium-dependent adenosine 5'-triphosphatase in sarcoplasmic reticulum: a detailed study

Restall¹,

Dale²,

Murray³

et al. 1984

Biochemistry

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The Ca2+-Mg2+ adenosine-5'-triphosphatase (ATPase) in sarcoplasmic reticulum has been covalently labeled with the phosphorescent triplet probe erythrosinyl 5-isothiocyanate. The rotational diffusion of the protein in the membrane at 25 degrees C was examined by measuring the time dependence of the phosphorescence emission anisotropy. Detailed analysis of both the total emission S(t) = Iv(t) + 2IH(t) and anisotropy R(t) = [Iv(t) - IH(t)]/[Iv(t) + 2IH(t)] curves shows the presence of multiple components. The latter is incompatible with a simple model of protein movement. The experimental data are consistent with a model in which the sum of four exponential components defines the phosphorescence decay. The anisotropy decay corresponds to a model in which the phosphor itself or a small phosphor-bearing segment reorients on a sub-microsecond time scale about an axis attached to a larger segment, which in turn reorients on a time scale of a few microseconds about an axis fixed in the frame of the ATPase. A fraction of the protein molecules rotate on a time scale of 100-200 microseconds about the normal to the bilayer, while the rest are rotationally stationary, at least on a sub-millisecond time scale.

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Protein rotational diffusion and lipid structure of reconstituted systems of Ca2+-activated adenosine triphosphatase

Cited by 44 publications

References 19 publications

Theoretical studies of phospholipid bilayers and monolayers. Perturbing probes, monolayer phase transitions, and computer simulations of lipid–protein bilayers

Theoretical studies of phospholipid bilayers and monolayers. Perturbing probes, monolayer phase transitions, and computer simulations of lipid–protein bilayers

Compartmentalization of ceramide signaling: physical foundations and biological effects

Rotational diffusion of calcium-dependent adenosine 5'-triphosphatase in sarcoplasmic reticulum: a detailed study

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