Abstract
Structural studies of TM domains of single-spanning (bitopic) membrane proteins are impeded by their instability, flexibility and heterogeneity. The new computational method TMDOCK allows reliable modeling of homodimers of transmembrane (TM) α-helices on a proteomic scale. 3D models of 2129 parallel homodimers formed by TM α-helices of bitopic proteins from six evolutionarily distant organisms were modeled by TMDOCK, verified through experimental data available for nearly 600 proteins, and included in the Membranome database (v.2.0) along with related information to facilitate structural and evolutionary analysis of bitopic proteins. http://membranome.org. almz@umich.edu. Supplementary data are available at Bioinformatics online.
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