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In den WarenkorbArtikelbeschreibung des Verkäufers
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Bestandsnummer des Verkäufers CX-9780854048519
- Titel
- Biophysical Chemistry
- Verlag
- RSC Publishing
- Erscheinungsjahr
- 2002
- Zustand
- New
- Einband
- HRD
- Sprache
- Englisch
- ISBN-10
- 0854048510
- ISBN-13
- 9780854048519
- Artikelgewicht
- 551 Gramm
In the post-genomic world, advances in the comprehension of cell behaviour will depend upon scientists deciphering the molecular basis of interactions between proteins and membranes. Bringing together contributions from chemists, biologists and physicists, Biophysical Chemistry: Membranes and Proteins demonstrates how multidisciplinary teams can gain insights into understanding complex biological systems. This book reflects both the scope and the interdisciplinary nature of the field, with topics including: modelling of biological systems; membrane structure and interactions; probing biomolecules; and channels and receptors. Full of stimulating articles and opinions, readers from academia and industry will welcome the wide range of coverage and the state-of-the-art science.
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Biophysical Chemistry
Membranes and Proteins
By Richard H. Templer, Robin LeatherbarrowThe Royal Society of Chemistry
All rights reserved.
Contents
I Probing Biological Molecules: Theory and Experiment,
Flow Oriented Linear Dichroism to Probe Protein Orientation in Membrane Environments A. Rodger, J. Rajendra, R. Mortimer, T. Andrews, J.D. Hirst, A.T.B. Gilbert, R. Marrington, T.R. Dafforn, D.J. Halsall, M. Ardhammar, B. Nordén, C.A. Woolhead, C. Robinson, T.J.T. Pinheiro, J. Kazlauskaite, M. Seymour, N. Perez and M.J. Hannon, 3,
Quantitative Protein Circular Dichroism Calculations N.A. Besley and J.D. Hirst, 20,
Probing Cellular Structure and Function by Atomic Force Microscopy M.A. Horton, P.P. Lehenkari and G.T. Charras, 31,
Physical Characterization of Wild Type and mnn9 Mutant Cells of Saccharomyces cerevisiae by Atomic Force Microscopy (AFM) A. Méndez-Vilas, I. Corbacho, M.L. González-Martín and M.J. Nuevo, 50,
Probing Supramolecular Organisation at Immune Synapses F.E. McCann, K. Suhling, L.M. Carlin, K. Eleme, K. Yanagi, P.M.W. French, D. Phillips and D.M. Davis, 58,
Probing the Structure of Viral Ion Channel Proteins: A Computational Approach W.B. Fischer and M.S.P. Sansom, 72,
The Impact of H2O2 on the Structure of Catalases by Molecular Modelling Methods S.G. Kalko, J.Ll. Gelpí and M. Orozco, 78,
Entropy in the Alignment and Dimerization of Class C G-Protein Coupled Receptors M.K. Dean, C. Higgs, R.E. Smith, P.D. Scott, R.P. Bywater, T.J. Howe and C.A. Reynolds, 85,
Electrostatic Stability of Wild Type and Mutant Transthyretin Oligomers S. Skoulakis and J.M. Goodfellow, 94,
Simulations of Human Lysozyme: Conformations Triggering Amyloidosis in 156T Mutant G. Moraitakis and J.M. Goodfellow, 103,
Collective Excitation Dynamics in Molecular Aggregates: Exciton Relaxation, Self-Trapping and Polaron Formation M. Dahlbom, W. Beenken, V. Sundström and T. Pullerits, 118,
Surprising Electro-magnetic Properties of Close Packed Organized Organic Layers – Magnetization of Chiral Monolayers of Polypeptide I. Carmeli, V. Shakalova, R. Naaman and Z. Vager, 136,
Barrier Crossing by a Flexible Long Chain Molecule – The Kink Mechanism K.L. Sebastian, 147,
II Proteins, Lipids and Their Interactions,
Lipid Interaction with Cytidylyltransferase Regulates Membrane Synthesis S. Jackowski and I. Baburina, 163,
Models and Measurements on the Monolayer Bending Energy of Inverse Lyotropic Mesophases A.M. Squires, J.M. Seddon and R.H. Templer, 177,
Hemolytic and Antibacterial Activities of LK Peptides of Various Topologies: A Monolayer and PM-IRRAS Approach S. Castano, B. Desbat, H. Wróblewski and J. Dufourcq, 191,
A Novel Approach for Probing Protein-Lipid Interactions of MscL, a Membrane-Tension-Gated Channel P.C. Moe and P. Blount, 199,
Folding of The α-Helical Membrane Proteins DsbB and NhaA D.E. Otzen, 208,
FhuA, an Escherichia coli Transporter and Phage Receptor P. Boulanger, L. Plançon, M. Bonhivers and L. Letellier, 215,
Morpholgical Aspects of in cubo Protein Crystallisation C. Sennoga, B. Hankamer, A. Heron, J.M. Seddon, J. Barber and R.H. Templer, 221,
Mobility of Proteins and Lipids in the Photosynthetic Membranes of Cyanobacteria C.W. Mullineaux and M. Sarcina, 237,
Partitioning and Thermodynamics of Chlordiazepoxide in n-Octanol/Buffer and Liposome System C. Rodrigues, P. Gameiro, S. Reis, J.L.F.C. Lima and B. De Castro, 243,
Distribution of Vitamin E in Model Membranes P.J. Quinn, 248,
Theory on Opening-up of Liposomal Membranes by Adsorption of Talin Y. Suezaki, 254,
Differential Scanning Calorimetry and X-Ray Diffraction Studies of Glycolipid Membranes O. Ces, J.M. Seddon, R.H. Templer, D.A. Mannock and R.N. McElhaney, 267,
Subject Index, 277,
CHAPTER 1
Probing Biological Molecules: Theory and Experiment
FLOW ORIENTED LINEAR DICHROISM TO PROBE PROTEIN ORIENTATION IN MEMBRANE ENVIRONMENTS
Alison Rodger, Jascindra Rajendra, Rhoderick Mortimer, Terrence Andrews, Jonathan D. Hirst, Andrew T.B. Gilbert, Rachel Marrington, Timothy R. Dafforn, David J. Halsall, Malin Ardhammar, Bengt Nordén, Cheryl A. Woolhead, Colin Robinson, Teresa J.T. Pinheiro, Jurate Kazlauskaite, Mark Seymour, Niuvis Perez, Michael J. Hannon
1 INTRODUCTION
Processes occurring on or in membranes are essential in most biological systems, and the study of these processes has been engendering an increasing interest for a long time, as has the creation of artificial lipid membrane systems. Studies of, for example, membrane transport and membrane protein function call for a thorough knowledge of molecular interactions within the membrane, between the lipids themselves and between lipids and other species (proteins, drugs, and ions). To this end, the locations and orientations of molecules bound to the membrane can give important information. However, to date no simple experimental method has been established to achieve this for membrane bound proteins. In this work we report the first flow linear dichroism (LD) study of proteins bound to liposomes. Flow LD of molecules bound to the bilayer of shear-deformed liposomes is one of the few direct methods potentially available for the study of the orientation of membrane guest molecules, provided that the molecules of interest have significant absorption in the visible and near-UV regions.
Linear dichroism is the difference in absorption of light polarised parallel to an orientation direction and light polarised perpendicular to that direction. The LD signal is related to the oscillator strength of a transition (its absorbance intensity) and the polarisation of the transition relative to the orientation axis. It is thus the ideal technique to use to probe the orientation of an analyte and it is widely used, for example, for determining the orientation of drugs bound to flow oriented DNA. The most effective method for achieving flow orientation has proved to be Couette flow where two concentric cylinders with a small annular gap (usually 500 µm) are aligned and one of them rotates. The light is incident radially on the cell so the stationary cylinder needs to have two windows and the rotating cylinder needs to be transparent to the intended radiation.
Liposomes can be considered models of cell membranes, and be used for studying transport and signal mechanisms of membrane proteins in situ. They are also used for drug delivery and as transfecting agents in gene therapy. Ardhammar, Mikati, Lincoln and Norden have shown that aromatic moieties or the aromatic 'arm' of ruthenium dipyridophenazine can be oriented in liposomes and their orientation detected when the liposomes are subjected to shear flow. In this work we probed the orientation achievable by flow with different size model membranes and then the application of LD to determine the orientation of proteins bound on or in liposomes. The proteins studied include gramicidin, cytochrome c, pre-PsbW (a thylakoid membrane protein precursor) and a monoclonal antibody.
2 LINEAR DICHROISM OF ANALYTES IN SHEAR DISTORTED LIPOSOMES
As noted above there are two literature precedents for flow orienting liposomes to assess the orientation of solutes in their bilayer. Ardhammar et al. found that pyrene and anthracene in soybean liposomes (produced by extrusion) had a negative...
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