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.
- April 23, 2012: Schedule for CMC Workshop and mini-Symposium now available
- April 17, 2012: Flexibility of the Flexizyme for in vitro incorporation of unnatural amino acids
- April 3, 2012: Frontiers in Membrane Protein Dynamics full schedule announced
- March 29, 2012: MPSDC-funded poster author wins Biophysical Society 2012 Student Research Achievement Award
- March 13, 2012: Computational Modeling Core to host Workshop and mini-Symposium on May 1st and 2nd View more entries »
May 3 & May 4, 2012
The Gleacher Center
450 North Cityfront Plaza Drive
Chicago, IL 60611
This conference consists of scientific sessions and poster presentations, and will feature both Consortium members and external invitees.
More information and schedule »
- Structural basis for iron piracy by pathogenic Neisseria (Published on March 1, 2012)
- Target-binding proteins based on the 10th human fibronectin type III domain (10Fn3) (Published on February 29, 2012)
- A gate-free pathway for substrate release from the inward-facing state of the Na(+)-galactose transporter (Published on February 1, 2012)
- Tracing cytoplasmic Ca2+ ion and water access points in the Ca2+-ATPase (Published on January 18, 2012) 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 in a given protein requires a molecular description of the types and extent of the protein movements underlying function. Read more »
By Robert Nakamoto
There is almost nothing more useful to the biophysicist than to have probes in known positions within the structure of a protein. Probe placement is most commonly done by site-directed mutagenesis to introduce a unique cysteine and chemically modifying the purified protein with a sulfhydryl-reactive label. Here, I describe a new and highly flexible method for synthesizing acyl-tRNA with a wide range of unnatural amino acids using the “Flexizyme”. Read more »
