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Biochimica et Biophysica Acta 1778 (2008) 1697 Contents lists available at ScienceDirect Biochimica et Biophysica Acta j o u r n a l h o m e p a g e : w w w. e l s ev i e r. c o m / l o c a t e / b b a m e m Preface Structural proteomics of the cell envelope of Gram-negative bacteria The cell envelope of Gram-negative bacteria, including the plasma membrane, the periplasmic space, and the outer membrane, can be viewed as a model organelle with a large number of diverse critical functions for bacterial physiology. A significant number of protein structures of both the inner and outer membrane, as well as proteins from the periplasm, have been solved by NMR or X-ray at an increasing rate over the past few years. Proteomics techniques have begun to make it possible to obtain a detailed inventory of the contents of the cell envelope of Gram-negative bacteria. The methods and data are now maturing to provide information about the interactions between the different proteins and other biomolecules. Biochemical and biophysical approaches have given a great deal of information about the cellular processes occurring in the envelope, including bioenergetics, transport, signaling, cell wall synthesis, and various other catalytic activities. The contributions in this special issue provide a timely review of major aspects of the envelope components with known structures and their environment. They complement the more microbiological approach in a recent book [1]. The degree of detail in our current understanding of the cell envelope and its processes suggests the cell envelope may become one of the first organelles that is sufficiently studied and understood to create computational models with predictive powers at a cellular level. Several reviews focus on individual classes of proteins, e.g., mechanosensitive channels and ABC transporters; others focus on 0005-2736/$ – see front matter © 2008 Elsevier B.V. All rights reserved. doi:10.1016/j.bbamem.2008.08.008 functional systems, such as the iron import cascade, protein secretion systems and the flagellar assembly; while yet others review the state of the art in methodological developments in crystallography, proteomics, and computational investigations in membrane proteins. We thank the authors of all contributions for their efforts. Reference [1] M. Ehrmann (Ed.), The Periplasm, American Society Microbiology, 2007. D. Peter Tieleman⁎ Raymond J. Turner Hans J. Vogel Department of Biological Sciences, University of Calgary, Calgary AB T2N1N4, Canada E-mail addresses: tieleman@ucalgary (D.P. Tieleman), [email protected] (R.J. Turner), [email protected] (H.J. Vogel). ⁎Corresponding author. Joel H. Weiner Department of Biochemistry, University of Alberta, Alberta, Canada E-mail address: [email protected] (J.H. Weiner).