Roland Glaser Professor Dr., David Gingell Professor Dr.'s Biophysics of the Cell Surface PDF

By Roland Glaser Professor Dr., David Gingell Professor Dr. (auth.), Roland Glaser Professor Dr., David Gingell Professor Dr. (eds.)

ISBN-10: 3642744710

ISBN-13: 9783642744716

ISBN-10: 3642744737

ISBN-13: 9783642744730

It is usual perform to post convention papers in books or monograph sequence. this offers a few virtue to people who didn't have the chance to wait the conferences, however it irritates and disappoints others who could have was hoping for a suite of heavily comparable studies. With this booklet now we have attempted to discover a compromise. It provides a variety from the subjects that have been mentioned in a chain of inter­ nationwide symposia entitled "Biophysics of mobile Surface", held in 1976, 1978, 1981, 1985 and 1988 within the GDR, and as a consequence released within the magazine STUDIA BIOPHYSICA (volumes fifty six, seventy four, ninety, a hundred and ten, 1271. approximately all of the members to this ebook participated in a single or extra of the conferences. we are hoping that our collection of issues chosen for this publication manages to mirror the range and curiosity of the wide diversity of topics which fall in the scope of membrane biophysics, with no taking over the randomness of a systematic car-boot sale. we wish to precise our due to all colleagues and organ~ isations who helped to gain the meetings and especially this ebook. monetary aid for the symposia of 1985 and 1988 used to be supplied via the IUPAB. a couple of issues, mirrored during this ebook, ended in internat­ ional cooperations, supported by way of a number of agencies. we're specifically thankful for the aid of UNESCO learn venture on biophysicS during this recognize. the ecu Bureau (ROSTE) of UNESCO supported the editorial paintings of this book.

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No changes were observed for choline lipid bilayers alone and all these studies were performed with lipid bilayers containing dimyristoyl acyl chains in the liquid crystalline phase. Although some spectral broadening was observed (no spin-spin relaxation time determinations were made) quadrupole splitting changes could be measured over a very wide range (from 1000:1 to 22:1, lipid:protein mole ratio) of protein concentrations. It appears, from the earlier determinations of available basic amino acid residues for phospholipid head group association from Mn++ binding studies (see above), that there is a one-for-one molecular association between a lipid and an amino acid binding of this protein to the membrane surface (Figure 7).

L1Vq(free) 37 where L\Vq(free) is the value for protein free bilayer unperturbed by the protein and can be determined directly. This can be rearranged to give: 1 L\vq(observed) = I1c(L\vq(complex) - L\Vq(free)). nt . + L\Vq(free) The stoichiometry (number of lipids in a lipid-protein complex, ne) can therefore be obtained in principle from the slope of the dependence of L\Vq(observed) with lint, the protein:lipid mole ratio. If it is assumed that the lipid head groups are totally disordered (or at least give a 2H-NMR spectrum with no measurable quadrupole splitting, ~Vq - 0) then a value for ne can be deduced; a value of ne - 21 - 35 lipids per protein was estimated from four independent sets of experimental results, those from three deuterated segments of the glycerol head group as well as the phosphorus spectral changes.

1986). , 1978). Possible contributing amino acid side groups are carboxylic acid side groups in this pH range since the surface. lysine amino groups would titrate at pH 9 - 10. In contrast, the acyl chain motion, as reported by the spin-label, does not change significantly in this range suggesting that the apparent change in binding may correspond to a change in the number of proteins bound rather than a wholesale displacement of the protein from the bilayer surface. Electron microscopy has been used to show that cytochrome c can induce the formation of lipidic particle~ in bilayers which are also revealed in 31P NMR studies as narrower isotropic spectral lines superimposed upon the more usual spherically averaged powder pattern from extended bilayers (De Kruijff and Cullis, 1980).

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Biophysics of the Cell Surface by Roland Glaser Professor Dr., David Gingell Professor Dr. (auth.), Roland Glaser Professor Dr., David Gingell Professor Dr. (eds.)

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