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 »

New webserver: prediction of LBT (lanthanide-binding tag) insertion onto membrane proteins

We have created a fully automated webserver for the prediction of LBT insertions onto existing protein structures. The method predicts the proper conformation of the LBT tag with respect to the parent protein in existing fusion crystal structures. We expect the method to serve as a useful computational tool for experimentalists by helping them select reasonable sites in a given parent protein where the LBT insertion will likely be successful. 

Learn more »
Structural Refinement Based on EPR Data from Restrained-Ensemble Simulation

Recently, a novel computational simulation technique was developed to exploit the information from distance distribution data obtained from ESR/DEER spectroscopy for the refinement of membrane protein structures. Read more »
Klaus Schulten's keynote lecture movie made available with audio
Following our earlier interview with Frontiers in Membrane Protein Structural Dynamics 2014 keynote lecturer Klaus Schulten, we have made available the fascinating movie “Photosynthetic Membrane of Purple Bacteria – A Clockwork of Proteins and Processes” which was shown during the lecture, now with Schulten's narrative.

Watch the video »