Abstract
Membrane proteins are critical to living cells and their dysfunction can lead to serious diseases. High-resolution structures of these proteins would provide very valuable information for designing eficient therapies but membrane protein crystallization is a major bottleneck. As an important alternative approach, methods for predicting membrane protein structures have been developed in recent years. This chapter focuses on the problem of modeling the structure of transmembrane helical proteins, and describes recent advancements, current limitations, and future challenges facing de novo modeling, modeling with experimental constraints, and high-resolution comparative modeling of these proteins. Abbreviations: MP, membrane protein; SP, water-soluble protein; RMSD, root-mean square deviation; Cα RMSD, root-mean square deviation over Cα atoms; TM, transmembrane; TMH, transmembrane helix; GPCR, G protein-coupled receptor; 3D, three dimensional; NMR, nuclear magnetic resonance spectroscopy; EPR, electron paramagnetic resonance spectroscopy; FTIR, Fourier transform infrared spectroscopy.
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Barth, P. (2010). Prediction of three-dimensional transmembrane helical protein structures. In: Structural Bioinformatics of Membrane Proteins. Springer, Vienna. https://doi.org/10.1007/978-3-7091-0045-5_13
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DOI: https://doi.org/10.1007/978-3-7091-0045-5_13
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