Structural Biology of Membrane Proteins
The past few years have seen exciting advances in the field of membrane protein structural biology. Although membrane proteins still constitute a small fraction of the total number of solved protein structures (see Hartmut Michel’s and Stephen White’s summaries at http://www.mpibp-frankfurt.mpg.de/michel/public/memprotstruct.html, http://blanco.biomol.uci.edu/Membrane_Proteins_xtal.html), an exponential increase of membrane protein structures has been observed1 and is anticipated to continue. This book addresses a number of issues pertaining to membrane protein structural biology. The first section describes approaches for expression and purification of membrane proteins, and a general introduction to detergents. The major challenge in this field is with eukaryotic membrane proteins, which is reflected by the contributions in this section. The second section addresses selected methods for structure determination of membrane proteins, such as solution and solid-state nuclear magnetic resonance, atomic force microscopy, electron microscopy including single particle analysis and lipidic cubic phase crystallization. The final section highlights some of the recently solved membrane protein structures. The content of the individual chapters varies from basic introduction to very detailed description of a particular theme. Therefore, the experienced membrane protein biochemist, as well as the novice, will find useful information. While we have endeavored to provide a balanced overview, not all topics could be covered. Clearly, this book is not an exhaustive reference for all concepts relating to membrane protein structural biology. However, the following paragraphs give some further information with key references on topics not addressed by this book. Heterologous expression and purification of membrane proteins have been covered by a number of reviews.2–5 Here, the reader will find information on both prokaryotic and eukaryotic membrane proteins. Until recently, all structures of eukaryotic membrane proteins, for example the visual pigment rhodopsin,6,7 had been solved with material from natural sources, reflecting the difficulty of producing functional eukaryotic membrane proteins in heterologous expression systems. The new structure of a recombinant mammalian voltage-gated potassium channel, produced in the yeast Pichia pastoris, is therefore exciting.8
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