Related Experiment Video
Updated: Feb 19, 2026
High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
Published on: October 15, 2019
Membranome 2.0: database for proteome-wide profiling of bitopic proteins and their dimers
Andrei L Lomize1, Jacob M Hage2, Irina D Pogozheva1
1Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, MI 48109-1065, USA.
Motivation:
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.
Results:
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.
Availability And Implementation:
http://membranome.org.
Contact:
almz@umich.edu.
Supplementary Information:
Supplementary data are available at Bioinformatics online.
