Membrane Proteins: Structures, Interactions and Models: by R. M. Glaeser (auth.), Alberte Pullman, Joshua Jortner,

By R. M. Glaeser (auth.), Alberte Pullman, Joshua Jortner, Bernard Pullman (eds.)

The twenty fifth Jerusalem Symposium represents a most vital spotlight within the improvement and background of those conferences. dwelling in the decimal approach we have now celebrated with a lot excitement the lath and the twentieth Jerusalem Symposia. With this one we event a sense of specific pride simply because 25 years isn't like, is greater than, twenty years and a part. it's a area of a century. it sort of feels hence as though we have now replaced the measurement of our endeavour. on no account can we unfastened the experience of modesty with admire to the importance of those conferences. For the organizers, in spite of the fact that, they do symbolize a continuity of efforts which we think chuffed to were capable of perform. At this celebration it kind of feels necessary to claim a number of phrases in regards to the beginning of the Jerusalem Symposia and to keep in mind the identify of a colleague who performed a vital function of their production and has been a best and committed co­ organizer of the seven first of them. This used to be Professor Ernst Bergmann, some of the most special founders of Israeli technology and an international recognized physico-organic chemist.

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Additional resources for Membrane Proteins: Structures, Interactions and Models: Proceedings of the Twenty-Fifth Jerusalem Symposium on Quantum Chemistry and Biochemistry Held in Jerusalem, Israel, May 18–21,1992

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1974). Studies of theoretical circular dichroism of polypeptides: Contributions of {J turns. In Peptides, Polypeptides and Proteins (Blout, E. , Bovey, F. , Goodman, M. , N. Y. Woody, R. W. , Jr. (1967). Optical rotation of oriented helices. III. Calculation of rotatory dispersion and circular dichroism of the alpha and 310 helix. J. Chern. Phys. , Nakazawa, T. and Nakazawa, A. (1982). Nucleotide sequence of the structural gene for colicin El and predicted structure of the protein. Proc. Natl.

2. 6% (w/v) octyl tetraoxyelhyleoe. 3 mM oodium azide; A-A. 1 M NoCI. 20 mM oodium phoopbate. 0. 2 mM EDTA. 1% OPOE. 2 mM OTT. odium azide; x-x. Phoaphoporin(l ma/mll in SO mM NoCI. 20 mM sodium phoopbate. 6. 9% fJoctyillucoaide. The CD speclnl were measured. u described in Fil. FiJ·4 Ciroular Dichroism apecInI of RhodopaiDs: 0_0. 72 ma/mll in O. IS M NoCI. IS mM oodium phoopbate. 6. 1 % Iowyl maltoaide; +-+. 15 M NaCl. 15 mM oodiumpboapbate. 6. 1% Iowyl maJtooide; 0-0. 95 ma/mll in water. The CD apecInI were meuured.

262,3768-3774 Brunden, K. , Vratani, Y. and Cramer, W. A. (1984). Dependence of the conformation of a colicin E1 channel-forming peptide on acidic Ph and solvent polarity. 1. BioI. , Norris, J. and Schiffer, M. (1986). Structure of Rhodopseudomonas sphaeroides R-26 reaction center. FEBS lett. 205, 82-86 Chang, C. -S. C. and Yang, J. T. (1978). Circular dichroism analysis of protein conformation: Inclusion of the (3-turns. Anal. Biochem. , Yang, J. T. and Chau, K. H. (1974). Determination of the helix and (3-form of proteins in aqueous solution by circular dichroism.

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