By Roland Glaser Professor Dr., David Gingell Professor Dr. (auth.), Roland Glaser Professor Dr., David Gingell Professor Dr. (eds.)
It is usual perform to post convention papers in books or monograph sequence. this offers a few virtue to those that 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 stories. With this ebook we've got attempted to discover a compromise. It offers a range from the subjects that have been mentioned in a chain of inter nationwide symposia entitled "Biophysics of telephone Surface", held in 1976, 1978, 1981, 1985 and 1988 within the GDR, and to that end released within the magazine STUDIA BIOPHYSICA (volumes fifty six, seventy four, ninety, a hundred and ten, 1271. approximately all of the participants to this booklet participated in a single or extra of the conferences. we are hoping that our collection of issues chosen for this booklet manages to mirror the range and curiosity of the extensive variety of topics which fall in the scope of membrane biophysics, with no taking up the randomness of a systematic car-boot sale. we wish to specific our because of all colleagues and organ~ isations who helped to achieve the meetings and especially this booklet. monetary help for the symposia of 1985 and 1988 was once supplied via the IUPAB. a few subject matters, mirrored during this booklet, led to internat ional cooperations, supported by means of a variety of businesses. we're in particular thankful for the help of UNESCO study undertaking on biophysicS during this recognize. the ecu Bureau (ROSTE) of UNESCO supported the editorial paintings of this book.
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Extra info for Biophysics of the Cell Surface
The functional significance of lipid-protein interactions are now well documented (Sandermann, 1986). Ganglioside GMI which is the receptor for cholera toxin, triggers the regulatory cascade involving adenylate cyclase and protein kinase (Moss and Vaughan, 1979) and gangliosides have more recently been shown to regulate cell growth by binding to an allosteric site on the epidermal growth factor receptor (Hakomori, 1979). , 1978). It has been suggested that kinetic cooperativity between lipids and protein activity can occur with two possible mechanisms, (i) allosteric control resulting from interaction at lipidprotein binding sites (which could be at the membrane surface) and (ii) non-allosteric mechanism requiring a lipid solvation shell around the protein (see Table 3 in: Sandermann, 1986).
The high affinity of myelin basic protein for acidic lipids was first demonstrated in a solvent complex (Palmer and Dawson, 1969) in which the relative association with bound lipids decreased upon acylation of the protein lysine residues. The protein has 31 basic amino acids (Lys, Arg) and 11 acidic residues (Asp, GIu) at physiological pH of a total of 170 amino acids thereby giving the protein its basic character (Boggs and Moscarello, 1978). The 52% 35 apolar residues, of which 24% are hydrophobic, suggest that this protein not only binds to membrane surfaces but also penetrates the hydrophobic core.
It forms heterodimers composed of two non-identical subunits (n chain, 240000 daltons, and ~ chain 220000 daltons). Each subunit is composed of several homologous triple helical segments (Speicher and Marchesi, 1984). Spectrin heterodimers participate in head-to-head association to form tetramers (Marchesi, 1983). 1 to form a meshwork. This meshwork is linked to the plasma membrane by association of spectrin with ankyrin, which, in turn, is associated to band 3 (Bennett, 1989). Besides its interaction with a number of other cytoske1etal proteins, spectrin is thought to have a direct association with the cytoplasmic surface of the lipid bilayer.