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Conformational Transitions and Alternating-Access Mechanism in the Sarcoplasmic Reticulum Calcium Pump
By Avisek Das, Huan Rui, Robert Nakamoto, Benoît Roux.
Published in J Mol Biol. 2017 Mar 10;429(5):647-666.… [more]
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Energy transduction and alternating access of the mammalian ABC transporter P-glycoprotein
By Brandy Verhalen, Reza Dastvan, Sundarapandian Thangapandian, Yelena Peskova, Hanane A. Koteiche, Robert… [more]
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Visualization of SNARE-Mediated Hemifusion between Giant Unilamellar Vesicles Arrested by Myricetin
By Paul Heo, Joon-Bum Park, Yeon-Kyun Shin, and Dae-Hyuk Kweon.
Published in Front Mol Neurosci. 2017… [more]
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CHARMM-GUI 10 years for biomolecular modeling and simulation
By Sunhwan Jo, Xi Cheng, Jumin Lee, Seonghoon Kim, Sang-Jun Park, Dhilon S. Patel, Andrew H. Beaven,… [more]
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The role of transmembrane segment 5 (TM5) in Na2 release and the conformational transition of neurotransmitter:sodium symporters toward the inward-open state
By Sebastian Stolzenberg, Zheng Li, Matthias Quick, Lina Malinauskaite, Poul Nissen, Harel Weinstein,… [more]
Welcome to the MPSDC Gateway!
Membrane proteins play an essential role in controlling the movement of material and information in and out of the cell, in determining the flow and use of energy, as well as in triggering the initiation of numerous signaling pathways. To fulfill these roles, conformational and interaction dynamics exert a dominant influence on their functional behavior, for it is the interplay between structure and dynamics what ultimately defines their function.
The Membrane Protein Structural Dynamics Consortium (MPSDC) has been designed as a highly interactive, tightly integrated and multidisciplinary effort focused on elucidating the relationship between structure, dynamics and function in a variety of membrane proteins. This website serves as a gateway both to the Consortium's activities and resources, and to the scientific field at large.
Read the director's statement »