عنوان

Membrane proteins :

شابک

9401052050

شابک

9401127182

شابک

9789401052054

شابک

9789401127189

شماره

b595115

عنوان اصلي

Membrane proteins :

نام عام مواد

[Book]

ساير اطلاعات عنواني

structures, interactions and models : proceedings of the twenty-fifth Jerusalem Symposium on Quantum Chemistry and Biochemistry held in Jerusalem, Israel, May 18-21, 1992

نام نخستين پديدآور

edited by Alberte Pullman, Joshua Jortner, Bernard Pullman.

محل نشرو پخش و غیره

Dordrecht

نام ناشر، پخش کننده و غيره

Springer Science+Business Media, B.V.

تاریخ نشرو بخش و غیره

1992

نام خاص و کميت اثر

(X, 506 p.).

عنوان فروست

Jerusalem symposia on quantum chemistry and biochemistry, Volume 25.

متن يادداشت

Bibliographic Level Mode of Issuance: Monograph.

متن يادداشت

Electron Crystallography of Membrane Proteins 1 --; High-Resolution Electron Microscopy of Membrane Proteins --; Distinguishing Transmembrane Helices from Peripheral Helices by Circular Dichroism --; High-Resolution NMR of Membrane Proteins: the Example of Bacteriorhodopsin --; Molecular Dynamics Simulations of Bacteriorhodopsin --; Dynamics of Bacteriorhodopsin Studied by Neutron Scattering: Effects of the Environment, Softness and Structure --; What do Neutrons, X-Ray Synchrotron Radiation, Optical pH-Indicators, and Mutagenesis tell us about the Light-Driven Proton Pump Bacteriorhodopsin ? --; From Time-Resolved Difference Spectra to Kinetics, Mechanism, and Thermodynamics in the Bacteriorhodopsin Photocycle --; Arginine 175 is Part of an Anion Binding Site in Bacteriorhodopsin --; Electrostatic Calculations of the pKa's of Ionizable Groups in Bacteriorhodopsin --; Dimerization of Glycophorin A Transmembrane Helices: Mutagenesis and Modeling --; The Nicotinic Acetylcholine Receptor, a Model of Ligand-Gated Ion Channels: Investigation of its Functional Organization by Protein Chemistry and Site-Directed Mutagenesis --; Molecular Evolution of the Binding Site of the Nicotinic Acetylcholine Receptor --; 3-D Structure of Acetylcholinesterase and Complexes of it with Anticholinesterase Agents --; Modelling and Mutagenesis of Butyrylcholinesterase Based on the X-Ray Structure of Acetylcholinesterase --; The Nicotinic Acetylcholine Receptor and its Lipid Microenvironment --; A Correlation Between Patch Clamp and Fluorescence Anisotropy Experiments to Study Alterations on the Acethylcholine Channel Induced by Cholesterol Enrichment in Chick Myocytes --; Interaction of the Nicotinic Acetylcholine Receptor with Ligands and Membrane Lipids Studied by Fourier-Transform Infrared Spectroscopy and Photoaffinity Labeling --; On the Complexation of the Methylammonium Ion by Aromatic Side Chains of Proteins --; The Inhibitory Glycine Receptor: Structure-Function Studies on a Neuronal Chloride Channel --; Determinants of Ligand Binding to the Inhibitory Glycine Receptor --; Channel Proteins: from Anatomy to Design --; Linking Permeation Behavior and Structure of Ion Channels with a Microscopic Model --; Molecular Structure-Function Relations in Voltage-Gated Ion Channels of Excitable Membranes --; A Novel Model for Saturation of Ion Conductivity in Transmembrane Channels --; Computational Approaches to Understanding the Ion Channel-Lipid System --; A Minimal Model of Ion Channels: Polyamino Acids in Liposomes --; Structure and Dynamics of Melittin in Solution and Membranes from Amide Hydrogen Exchange Analysis --; Computer Modelling of Ion Binding Sites in Proteins --; Sec-Dependent and Sec-Independent Mechanisms of Protein Insertion into Bacterial Membranes --; Puncturing Cell Membranes: Comparison of Colicin A and Aerolysin --; Structure-Function Relationships in the Membrane Channel Porin as Based on a 1.8 A Resolution Crystal Structure --; Molecular Mechanism of Action of Pore-Forming Colicins and of their Immunity Proteins --; Preliminary Structural Studies of Photosystem I --; Problems and Progress in Computational Approaches to the Molecular Basis of Recognition --; Assembly of Escherichia Coli Inner Membrane Proteins: Sec-Dependent and Sec-Independent Membrane Insertion --; Molecular Dynamics Simulations of Phospholipid Membranes and their Interaction with Phospholipase A2 --; Electron Transfer in Bacterial Photosynthetic Reaction Centers --; Proton Transfer Pathways in Photosynthetic Reaction Centers Studied by Site-Directed Mutagenesis.

متن يادداشت

The 25th Jerusalem Symposium represents a most significant highlight in the development and history of these meetings. Living within the decimal system we have celebrated with much pleasure the lath and the 20th Jerusalem Symposia. With this one we experience a feeling of particular satisfaction because 25 years is different from, is more than, two decades and a half. It is a quarter of a century. It seems thus as if we have changed the dimension of our endeavour. In no way do we loose the sense of modesty with respect to the significance of these meetings. For the organizers, however, they do represent a continuity of efforts which we feel happy to have been able to carry out. At this occasion it seems useful to say a few words about the origin of the Jerusalem Symposia and to recall the name of a colleague who played an essential role in their creation and has been a most efficient and devoted co­ organizer of the seven first of them. This was Professor Ernst Bergmann, one of the most distinguished founders of Israeli Science and a world famous physico-organic chemist.

موضوع مستند نشده

Membrane proteins -- Congresses.

موضوع مستند نشده

Membrane proteins.

مستند نام اشخاص تاييد نشده

edited by Alberte Pullman, Joshua Jortner, Bernard Pullman.

مستند نام اشخاص تاييد نشده

Alberte Pullman

مستند نام اشخاص تاييد نشده

Bernard Pullman

مستند نام اشخاص تاييد نشده

Joshua Jortner

نام الکترونيکي

نوع ماده

[Book]

تكميل شده

Y