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.
- May 22, 2013: Consortium progress and scientific advances discussed at third annual meeting
- May 6, 2013: Workshop on Computational Modeling on May 7th
- May 3, 2013: Mini-Symposium on Computational Approaches on May 8th
- April 23, 2013: Workshop on Membrane Protein Production on May 8th
- April 23, 2013: Collaborative MPSDC team develops innovative computational simulation technique
- April 16, 2013: Overview: Structural Refinement Based on EPR Data from Restrained-Ensemble Simulation View more entries »
This software, developed by H. Clark Hyde of Francisco Bezanilla's group in 2012, allows accurate 3D positioning and inter-probe distance estimation in functional homomeric proteins. SNPS determines the 3D position of lanthanide donors attached to a target site, relative to a fluorescent acceptor placed in a reference site.
- A novel mechanism for fine-tuning open-state stability in a voltage-gated potassium channel (Published on April 30, 2013)
- Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide (Published on April 21, 2013)
- Structural Refinement from Restrained-Ensemble Simulations Based on EPR/DEER Data: Application to T4 Lysozyme (Published on April 12, 2013)
- Restrained-Ensemble Molecular Dynamics Simulations Based on Distance Histograms from Double Electron-Electron Resonance Spectroscopy (Published on March 19, 2013) View more entries »
The functional behavior of most proteins is intimately related to their conformational dynamics. It follows that a thorough understanding of structure-function relations requires a molecular description of the types and extent of the protein movements underlying function.
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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 »
