Sunday, August 18, 2013
Wednesday, March 20, 2013
No more rooms!
We have run out of rooms at Camp Allen, which means we cannot accept any more registations from people who need housing.
Sunday, February 3, 2013
Saturday, May 19, 2012
Same meeting, new name
After 20 years of explaining that it's not just for protein folding, we've decided to change the name of the meeting to the Texas Folding and Function Meeting. The 21st meeting will be on March 22-24, 2013. Save the dates!
21st Annual Texas Protein Folding and Function Meeting
Save the date!
21st Annual Texas Protein Folding and Function Meeting
March 22-24, 2013Keynote Speakers:
Keith Dunker, Indiana University School of Medicine
Dr. Keith Dunker and his collaborators first recognized intrinsically disordered proteins as a distinct protein class with important biological functions. His research includes improving disorder prediction algorithms, correlating different types of disordered proteins with protein function, understanding the role of disorder in protein-protein and protein-nucleic acid interactions, and discovering the role of disorder in the evolution of the original proteins on earth.
Vijay Pande, Stanford University
The Pande lab uses physical simulation and Bayesian statistics / machine learning techniques to investigate protein folding at long time scales with the goal of predicting all possible experimental observables. In related projects, the Pande lab uses computational tools to probe the structure and stability of misfolded protein aggregates and small molecule binding / drug efficacy.
Thursday, April 5, 2012
Monday, March 26, 2012
2012 Keynotes
We will have three Keynotes for the 2012 meeting
Wah Chiu
Elizabeth Goldsmith
Jose Onuchic
Dr. Onuchic has led the biological physics community as it attempts to devise an integrated picture of a variety of model biochemical and biological systems. His research has expanded across the scales of molecular-level interactions to cellular systems to organized multi-cellular structures. At Rice he will move this view towards medical applications focusing on cancer. In protein folding, he has introduced the concept of protein folding funnels as a mechanism for the folding of proteins. Convergent kinetic pathways, or folding funnels, guide folding to a unique, stable, native conformation. Energy landscape theory and the funnel concept provide the theoretical framework needed to pose and to address the questions of protein folding and function mechanisms. He also works on the theory of chemical reactions in condensed matter with emphasis on biological electron transfer reactions. He is now broadening his interests to stochastic effects in genetic networks.
Dr. Wah Chiu's laboratory has pioneered various experimental and computational methods in biological cryo-EM. His group has determined cryo-EM structures of biological bundle, ion channel, viruses and chaperonins at unprecedented resolutions. This includes the capability of tracing Ca backbone of protein components in several large molecular nanomachines using single particle cryo-EM without the aid of crystallography. Many of Dr. Chiu's structural investigations have produced not only novel structural informatics but also insightful functional mechanisms on protein folding and virus infection respectively.
Dr. Goldsmith's laboratory studies how signal transducing proteins are regulated by protein conformational changes. The ubiquitous protein kinase family of signaling proteins offers rich diversity in regulatory mechanisms. With her collaborator, Melanie Cobb, the structures of the first pair of active and inactive kinase structures that of the phosphorylated and unphosphorylated MAP kinase ERK2 were solved. They continue to study MAP kinase pathway enzymes and have recently solved the structure of the MAP3K TAO2. A second focus of the Lab is on the serpin family of protease inhibitors. These molecules undergo the most dramatic conformational changes presently known to occur in proteins. These changes function in the activity of serpins to inhibit and clear target proteases from the blood. The conformational changes are irreversible, and reflect the irreversible pathway in which they function. We are interested in locating other proteins that might have the feature of irreversible conformational changes functioning in either cell division or apoptosis.
Wah Chiu
Elizabeth Goldsmith
Jose Onuchic
Dr. Onuchic has led the biological physics community as it attempts to devise an integrated picture of a variety of model biochemical and biological systems. His research has expanded across the scales of molecular-level interactions to cellular systems to organized multi-cellular structures. At Rice he will move this view towards medical applications focusing on cancer. In protein folding, he has introduced the concept of protein folding funnels as a mechanism for the folding of proteins. Convergent kinetic pathways, or folding funnels, guide folding to a unique, stable, native conformation. Energy landscape theory and the funnel concept provide the theoretical framework needed to pose and to address the questions of protein folding and function mechanisms. He also works on the theory of chemical reactions in condensed matter with emphasis on biological electron transfer reactions. He is now broadening his interests to stochastic effects in genetic networks.
Dr. Wah Chiu's laboratory has pioneered various experimental and computational methods in biological cryo-EM. His group has determined cryo-EM structures of biological bundle, ion channel, viruses and chaperonins at unprecedented resolutions. This includes the capability of tracing Ca backbone of protein components in several large molecular nanomachines using single particle cryo-EM without the aid of crystallography. Many of Dr. Chiu's structural investigations have produced not only novel structural informatics but also insightful functional mechanisms on protein folding and virus infection respectively.
Dr. Goldsmith's laboratory studies how signal transducing proteins are regulated by protein conformational changes. The ubiquitous protein kinase family of signaling proteins offers rich diversity in regulatory mechanisms. With her collaborator, Melanie Cobb, the structures of the first pair of active and inactive kinase structures that of the phosphorylated and unphosphorylated MAP kinase ERK2 were solved. They continue to study MAP kinase pathway enzymes and have recently solved the structure of the MAP3K TAO2. A second focus of the Lab is on the serpin family of protease inhibitors. These molecules undergo the most dramatic conformational changes presently known to occur in proteins. These changes function in the activity of serpins to inhibit and clear target proteases from the blood. The conformational changes are irreversible, and reflect the irreversible pathway in which they function. We are interested in locating other proteins that might have the feature of irreversible conformational changes functioning in either cell division or apoptosis.
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