Bethesda, MD The Biophysical Society has announced the speakers for the New and Notable Symposium at the Joint Meeting of the Biophysical Society and the International Biophysics Congress in Long Beach, California, February 2-6, 2008. The new and notable symposium highlights the latest and most exciting discoveries in biophysics. Speakers are nominated and selected by the Societys program committee. The session will take place Tuesday February 5, 2008 from 4:00-6:00 PM in Ballroom 1 of the Long Beach Convention Center. Registration for the meeting is required.
New and Notable Symposium Speakers and Information:
The Effect of Chaperone SecB on MBP Folding: A Single-molecule Study.
Sander J. Tans, AMOLF institute, Amsterdam, the Netherlands.
Dr. Tans has conducted the first experimental study to show how a chaperone affects a protein folding pathway. The chaperone was shown to interfere specifically with some folding transitions, and to prevent protein aggregation. Laser tweezers combined with MD simulations enabled these single molecule investigations. Studies of folding pathways have so far mainly focused on proteins in isolation. Protein misfolding and aggregation is thought to cause Alzheimers disease, for instance. This work was recently published in Science.
The Kinesin13-microtubule Complex.
Hernando Sosa, Albert Einstein College of Medicine.
Dr. Sosa has recently obtained a 3D map by cryo-electron microscopy and helical reconstruction of the kinesin-13 motor domain interacting with microtubules. The structure is very different from other kinesin-microtubule complexes. It shows the kinesin13 motor domain interacting with a curved protofilament and reveals a new microtubule binding site on the notor domain. This is the first 3D cryo-em map revealing the interaction of the kinesin-13 motor domain with a curved protofilament and provides a snapshot of the depolymerization cycle.
High-resolution Structure of the Human beta2-adrenergic Receptor.
Vadim Cherezov, The Scripps Research Institute.
Dr. Cherezov has solved the first high-resolution structure of a human G protein-coupled receptor with a diffusible ligand. This breakthrough represents the initial step in elucidating structural aspects of the ligand binding specifity and the mechanism of signal transduction by this diverse family of human druggable receptors. This is a major breakthrough that could only have been realized with the conjunction of the in meso method for membrane protein crystallization, a novel synchrotron X-ray beam and a suitably engineered protein. The target protein is of great biological and medical relevance.
Determining the Architectures of Macromolecular Assemblies by Integrating Spatial Restraints from Proteomic Data.
Frank Alber, University of Sounther California.
Dr. Alber has devised an integrative approach to determine the architectures of macromolecular assemblies from diverse biophysical and proteomic data. By applying this approach, he and his colleagues have determined the configuration of the 456 proteins in the nuclear pore complex (NPC) and gained insights into the assembly's evolution and architectural principles. The NPC controls the access of macromolecules in and out of the cell nucleus. The approach can, in principle, be applied to resolve the architectures of many other macromolecular complexes.
For more information or press credentials, contact Ellen Weiss at eweiss@biophysics org, or stop by the Society office located in the Room 103A of the Long Beach convention center.
|Contact: Ellen R. Weiss|