The Membrane Protein Structural Dynamics Consortium (MPSDC) is a highly interactive, tightly integrated and multidisciplinary effort focused on elucidating the relationship between structure, dynamics and function in a variety of membrane proteins. The Consortium has been in existence since 2010 and is funded by an NIH/NIGMS Glue Grant, which promote large-scale collaborative approaches to solve complex problems in biomedical science. A complete list of MPSDC institutions and their locations is available on the Participating Institutions page.
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 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. Our team continues to study major mechanistic questions associated with membrane protein function as it
relates to two major areas: energy transduction in signaling (ion channels and receptors) and energy interconversion (transporters and pumps).
To accomplish its goals, the MPSDC is developing a set of tools, concepts and reagents to:
1) Apply state of the art spectroscopic methods (Magnetic Resonance, Fluorescence, 2D-IR) to follow conformational changes and dynamics of the determined structures and generate a basis set of conformational transitions studies under a wide window of dynamics sampling.
2) Correlate dynamic measurements with high-resolution ensemble and single molecule functional measurements
3) Design and implement novel computational approaches to link the generated (and available) static and dynamic data with function.
Though originally designed to be organizationally flexible and fluid, the current iteration of MPSDC is formed by three scientific core facilities, which feed and interconnect with individual projects in a highly interactive way. These cores are designed to act as both, “innovation incubators” and research support centers by providing service and expertise in these critical areas: Membrane protein expression, the establishment of chemical synthesis capabilities for probes and detergents, the generation of a variety of binders and other crystallization chaperones and other target binders and the development of common computational tools to interpret and integrate the wealth of experimental data. Ultimately, our goal is to decode the mechanistic principles that govern protein movement and its associated fluctuation dynamics by dissecting the molecular and dynamic bases of these functions at an unprecedented and quantitative level.