Editorial: Special Issue on Membrane Proteins Biophysics

CARRER, D. C.

CURRENT PROTEIN AND PEPTIDE SCIENCE

BENTHAM SCIENCE PUBL LTD

Lugar: Bussum; Año: 2011 vol. 12 p. 684 - 684

1389-2037

One third of the genome of any organism encodes intrinsic membrane proteins. Along with peripheral membrane proteins and proteins that only transiently interact with the membrane, these molecules are hard to study but of great importance to understand both the normal and pathological life of the cell. Biophysical methods are of the utmost importance when trying to unravel the molecular details of processes that have been described by biochemical methods. In particular, biophysical methods are particularly well suited to study membrane proteins. We present here a sample of current understanding of membrane-associated proteins function and structure, studied by state-of-the-art biophysical, biochemical and modeling techniques. In the manuscript by Borioli, a novel hypothesis about immediate-early proto-oncoproteins structure-function relationship in regard to their ability to transiently interact with membranes is discussed. Colombo and Fasana discuss recent data regarding the unassisted insertion of tail-anchored proteins into the membrane of the endoplasmic reticulum. Cybulski and de Mendoza’s manuscript stresses the importance of bilayer thickness for membrane protein function. We present four manuscripts that use single-molecule methods to understand membrane-protein, protein-protein and carbohydrate-protein interactions in membranes, highlighting the increasing importance of these techniques for the development of the field. The manuscript by Bleicken and co workers describes the use of Fluorescence Correlation Spectroscopy to address the experimentally challenging study of the interaction between membrane proteins as they find each other in the bilayer. Clausen and Lagerholm discuss in detail the effect of the probe size and photophysics in the results obtained from single particle tracking of probes attached to membrane components. Ruprecht and co workers present a new way to analyze single molecule diffusion in the absence of a full analytical treatment. The method is based on the comparison of an experimental data set against the outcome of multiple experiments performed on the computer by Monte Carlo simulations. The manuscript by Leckband emphasizes the unique information obtained by force measurements on the binding mechanisms of lectins to cell-surface carbohydrates. Finally, Banning and co-authors summarize the recent findings on Reggie/Flotillin mechanisms of association in membrane microdomains and in oligomers. I am excited to deliver this issue that tackles a diverse set of developments in the area of the biophysics of membrane-associated proteins. I hope that it will be interesting for biophysicists, cell biologists and biochemists. I would like to thank all the authors who made this issue possible. I am in great debt to the anonymous reviewers from around the world who delivered timely and useful comments to the authors. I used here a double-blind method which I hope contributed to make the reviewing process more objective than it usually is. I also express my gratitude to the Editor-in-Chief Prof. Ben M. Dunn for his invitation and kind support that resulted in the successful completion of this special issue. Last but not least, a message of gratitude to the Assistant Manager of Bentham Science Publishers Sadia Rafique, who helped me with great efficiency to put together all the last details of the issue.