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Biomembranes structure

Chapman, D. (Ed.), Biomembrane Structure and Function, Vol. 4 of Topics in Molecular and Structural Biology, Verlag Chemie, Weinheim, 1984. [Pg.464]

Rohmer, M., P. Bouvier, and G. Ourisson. 1979. Molecular evolution of biomembranes structural equivalents and phylogenetic precursors of sterols. Proc. Natl. Acad. Sci. USA 76 847-851. [Pg.29]

Edwards JC, Chapman D, Cramp WA, Yatvin MB (1984) The effects of ionizing radiation on biomembrane structure and function. Progr Biophys Molec Biol 43 71-93 Eley DD, Spivey Dl (1962) Semiconductivity of organic substances. J Chem Soc Faraday Trans 58 411-415... [Pg.456]

Amberger HD, Fischer RD, Rosenbauer GG (1975) Ber Bunsenges Phys Chem 79 1226 Amcy RL, Chapman D (1983) In Chapman D (cd) Biomembranes Structure and Functions. McMillan Press, London, Chapt 4, p 199... [Pg.712]

Bach D (1983) In Chapman D (ed) Biomembrane Structure and Function. Verlag Chemie, Chapt... [Pg.713]

Verdieck JF, Peterson SH, Savage CM, Maker PD (1970) Chem Phys Lett 7 219 Verma SP, Wallach DFH (1983) In Chapman D (ed) Biomembrane Structure and Function. Verlag Chemie, p 167... [Pg.760]

Fyfe, P. K., McAuley-Hecht, K. E., Jones, M. R., and Cogdell, R. J., 1998a, Purple bacterial photosynthetic reaction centres. In Biomembrane Structures, (P. I. Haris and D. Chapman, eds.) 64987, lOS Press, Amsterdam, The Netherlands. [Pg.668]

Amey, R. L. and Chapman, D. Infrared spectroscopic studies of model and natural biomembranes. In Biomembrane Structure and Function. D. Chapman, ed. Verlag Chemie, 1989. [Pg.149]

Zinc atoms in some of the enzyme molecules participate in catalysis and also appear to be essential for maintenance of structmre of apoen-zymes. Zinc also plays a role in stabilization of biomembrane structure and polynucleotide conformation. Inasmuch as zinc appears to have a protective influence in hepatic cellular damage induced by carbon tetrachloride poisoning, it is reasonable to suggest that zinc also may have a direct effect on free radicals. [Pg.223]

O. S. Andersen, D. B. Sawyer and R. E. Koeppe, Modulation of channel function by host bilayers, in Biomembrane Structure and Function (eds B. Baber and K. R. K. Easwaran) p. 227. Adenine Press, Schenectady, 1992. [Pg.124]

The modem view of biomembrane structure is that it consists of an asymmetric Upid bilayer having proteins, both intrinsic and extrinsic, associated with it. The intrinsic proteins are embedded within and can span the bilayer [1-5]. Associated with this view of biomembrane structure is the idea that in many cases the Upid matrix can be in a fluid condition where the Upids are essentially above their transition temperatures (7J.) and able to diffuse within the bilayer matrix. An additional feature of certain biomembrane systems is the presence of cholesterol. [Pg.151]

Membrane structures that contain the visual receptor protein rhodopsin were formed by detergent dialysis on platinum, silicon oxide, titanium oxide, and indium—tin oxide electrodes. Electrochemical impedance spectroscopy was used to evaluate the biomembrane structures and their electrical properties. A model equivalent circuit is proposed to describe the membrane-electrode interface. The data suggest that the surface structure is a relatively complete single-membrane bilayer with a coverage of 0.97 and with long-term stability/... [Pg.485]

Figure 16. A schematic diagram of biomembrane structure (a cross section normal to the membrane surface), showing the charged hydrophilic amino acid side groups projecting into the aqueous phase and the uncharged hydrophobic groups in contact with the lipid phase of the bilayer. Figure 16. A schematic diagram of biomembrane structure (a cross section normal to the membrane surface), showing the charged hydrophilic amino acid side groups projecting into the aqueous phase and the uncharged hydrophobic groups in contact with the lipid phase of the bilayer.
The vital role played by phosphohpids in many biological processes has stimulated a number of studies concerning their chemistry, biochemistry, and physical properties. Phosphohpid analogues were found to be valuable tools in studies concerning elucidation of the mechanism of some enzymatic reactions [231], in probing biomembrane structures [232], and in the preparation of hposomes with the desired properties [233]. Phosphohpids have been used as drug carriers [234] or as drugs [233,235]. [Pg.177]

Organ and tissue implants Cell fractionation Probes of biomembrane structure Cell fractionation Cell fusion Endoeytosis Drugs Food additives Agricultural chemicals Cosmetics... [Pg.344]

Salamon Z and Tollin G (1998) Surface plasmon spectroscopy A new biophysical tool for probing membrane structure and function. In Chapman D and Haris P (eds) Biomembrane Structure. Amsterdam lOS Press. [Pg.1136]

Relatively few single crystal structures have been obtained of phospholipids, but those which are known reveal the same major structural features. The results are of direct relevance to biomembrane structure since phospholipids crystallize in bilayers and the characteristic features of the molecular structure are preserved in fully hydrated, fluid phospholipid bilayers. [Pg.132]

In the search for new substances to protect cells against external environmental effects such as UV radiation, some research has centered on the study of organisms capable of surviving under extreme conditions. These studies show that certain halophilic bacteria, such as Ectothiorhodospira halochloris, contain molecules (ectoins) capable of protecting cells against extreme conditions, maintaining osmotic equilibrium and stabihzing the protein, nucleic acid and biomembrane structures (Beyer, 20(X)). [Pg.384]


See other pages where Biomembranes structure is mentioned: [Pg.238]    [Pg.335]    [Pg.217]    [Pg.3]    [Pg.673]    [Pg.324]    [Pg.151]    [Pg.271]    [Pg.607]    [Pg.323]    [Pg.335]    [Pg.398]    [Pg.405]    [Pg.430]    [Pg.343]    [Pg.344]    [Pg.123]    [Pg.426]    [Pg.2038]    [Pg.2038]   
See also in sourсe #XX -- [ Pg.184 ]

See also in sourсe #XX -- [ Pg.184 ]

See also in sourсe #XX -- [ Pg.3 , Pg.2038 ]




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