ZIB

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

A small protein in model membranes: a time-resolved fluorescence and ESR study on the interaction of M13 coat protein with lipid bilayers (1992)

Sanders, Johan C. ; Ottaviani, M. Francesca ; Hoek, Arie ; [et al.]

Springer

European biophysics journal 21 (1992), S. 305-311

add to mindlist on the mindlist

Details

ISSN: 1432-1017

Keywords: M13 coat protein ; Lipid protein interaction ; ESR spectroscopy ; Time-resolved fluorescence spectroscopy ; Order parameter ; Diffusion coefficient

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Physics

Notes: Abstract Model membranes with unsaturated lipid chains containing various amounts of M13 coat protein in the α-helical form were studied using time-resolved fluorescence and ESR spectroscopy. The lipid-to-protein (L/P) ratios used were 〉 12 to avoid protein-protein contacts and irreversible aggregation leading to β-polymeric coat protein. In the ESR spectra of the 12-SASL probe in dioleoyl phosphatidylcholine (DOPC) bilayers no second protein induced component is observed upon incorporation of M13 coat protein. However, strong effects are detected on the ESR lineshapes upon changing the protein concentration. The ESR lineshapes are simulated by assuming a fixed ratio between the parallel (D‖) and perpendicular (D⊥) diffusion coefficients of 4, and an order parameter equal to zero. It is found that increasing the protein concentration from L/P ∞ to L/P 15 results in a decrease of the rotational diffusion coefficient D⊥ from 3.4 × 107 to 1.9 × 107 s−1. In the time-resolved fluorescence experiments with DPH-propionic acid as a probe, it is observed that increasing the M13 coat protein concentration causes an increase of the two fluorescent lifetimes, indicating an increase in bilayer order. Analysis of the time-resolved fluorescence anisotropy decay allows one to quantitatively determine the order parameters 〈P2〉 and 〈P4〉, and the rotational diffusion coefficient D⊥ of the fluorescent probe. The order parameters 〈P2〉 and 〈P4〉 increase from 0.34 to 0.55 and from 0.59 to 0.77, respectively, upon adding M13 coat protein to DOPC bilayers with an L/P ratio of 35. The rotational diffusion coefficient D⊥ of the DPH-propionic acid probe decreases on incorporating M13 coat protein, in accordance with the ESR results. It is concluded that M13 coat protein in the α-monomeric state is not able to produce a long living lipid boundary shell and consequently an immobilization of the lipids. An overall effect on the lipids is induced, resulting in a reduction in the dynamics and an increase in average lipid order. The hydrophobic region of M13 coat protein is proposed to perfectly match the lipid bilayer, resulting in a relatively small distortion of the bilayer structure of the lipid system.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00188342

Permalink

Library	Location	Call Number	Volume/Issue/Year	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Nitrogen hyperfine splitting of nitroxide solutions: Differently structured and charged nitroxides as probes of environmental properties (1987)

Ottaviani, M. Francesca ; Martini, Giacomo ; Nuti, Laura

Chichester : Wiley-Blackwell

Organic Magnetic Resonance 25 (1987), S. 897-904

add to mindlist on the mindlist

Details

ISSN: 0749-1581

Keywords: Nitroxides ; Nitrogen isotropic coupling constants ; Solvent polarity ; ESR spectra ; Chemistry ; Analytical Chemistry and Spectroscopy

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The dependence of the nitrogen isotropic coupling constants, aN, on the structure and charge of the radicals, temperature and solvent polarity was analysed for solutions containing the following nitroxides: 4-hydroxy-2,2,6,6-tetramethylpiperidine-1-oxyl (Tempol); 4-trimethylammonium-2,2,6,6-tetramethylpiperidine-1-oxyl, iodide salt (TempTMA+); 2,2,5,5-tetramethylpyrrolin-1-oxyl-3-carboxamide (Tempyo); and 2,2,5,5-tetramethylpyrrolin-1-oxyl-3-carboxylate, sodium salt (Tempyca-). Polar hydrogen bond acceptor solvents and hydroxylic solvents were used. In each solvent used, Tempol and Tempyca- showed aN values which were higher, respectively, than those of TempTMA+ and Tempyo due to inductive, structural and charge effects. Such effects were analysed on the basis of the proton and 13C coupling constants. Non-hydroxylic solvents gave temperature coefficients for aN that were almost independent of solvent polarity. Lower daN/dT values were found for charged radicals. A gradual decrease of temperature coefficients with decreasing hydrogen bond donor (HBD) properties were related to free volume changes of radical molecules. The analysis of the aN dependence on polarity parameters gave the best fitting using a simplified form of the Wertheim reaction field. Tempyca- was greatly affected by changes in polarity. A parameter to account for HBD abilities was also analysed.

Additional Material: 4 Ill.