Chapter title |
Solution NMR Studies of Integral Polytopic α-Helical Membrane Proteins: The Structure Determination of the Seven-Helix Transmembrane Receptor Sensory Rhodopsin II, pSRII.
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Chapter number | 3 |
Book title |
Membrane Protein Structure and Dynamics
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Published in |
Methods in molecular biology, August 2012
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DOI | 10.1007/978-1-62703-023-6_3 |
Pubmed ID | |
Book ISBNs |
978-1-62703-022-9, 978-1-62703-023-6
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Authors |
Gautier A, Nietlispach D, Gautier, Antoine, Nietlispach, Daniel, Antoine Gautier, Daniel Nietlispach |
Abstract |
About 30% of the proteins encoded in the genome are expressed as membrane proteins but these represent <1% of all the structures solved today. In view of the physiological and pharmaceutical significance of membrane proteins it is clear that a better and more comprehensive understanding of their three-dimensional (3D) structures at atomic resolution is required. α-Helical integral membrane proteins are generally more difficult to work with than β-barrel-type proteins and this has particularly been true for the polytopic members such as the large family of seven-helical proteins. In this chapter we describe the practical aspects of the solution-state NMR spectroscopy structure determination of the seven-helical transmembrane (7-TM) protein receptor sensory rhodopsin pSRII from the haloalkaliphilic archaeon Natronomonas pharaonis reconstituted in detergent micelles. This is the first time that a three-dimensional structure of a 7-TM protein has been determined by NMR. |
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