Bulletin of the American Physical Society
2007 APS March Meeting
Volume 52, Number 1
Monday–Friday, March 5–9, 2007; Denver, Colorado
Session T5: Simplifying Biological Complexity
Sponsoring Units: DBPChair: Per-Anker Lindgard, Risoe National Laboratory
Room: Colorado Convention Center Korbel 1A-1B
Wednesday, March 7, 2007 5:30PM - 6:06PM |
T5.00001: Statics and dynamics of ecosystems Invited Speaker: Understanding an ecological community represents a formidable many-body problem - one has an interacting many-body system with imperfectly known interactions and a wide range of spatial and temporal scales. In tropical forests across the globe, ecologists have been able to measure certain quantities such as the distribution of relative species abundance; the probability that two trees drawn randomly a specified distance apart belong to the same species; and the dynamics of species turnover. A simple analytic framework will be presented for describing the statics and dynamics of ecosystems and its predictions will be benchmarked against observational data. \newline \newline I. Volkov et al., Nature 424, 1035-1037 (2003); Phys. Rev. Lett. 92, 218703 (2004); Nature 438, 658-661 (2005). \newline T. Zillio et al., Phys. Rev. Lett. 95, 098101 (2005). \newline S. Azaele et al., Nature (2006) in press. [Preview Abstract] |
Wednesday, March 7, 2007 6:06PM - 6:42PM |
T5.00002: Mechanochemical cycles in cells Invited Speaker: |
Wednesday, March 7, 2007 6:42PM - 7:18PM |
T5.00003: Stretching to Understand Proteins Invited Speaker: Mechanical stretching of single proteins has been studied experimentally for about 50 proteins yielding a variety of force patterns and values of the peak forces. We have performed a theoretical survey of 7749 proteins of known native structure and map out the landscape of possible dynamical behaviors unders stretching at constant speed. The model used is constructed based on the native geometry. It is solved by methods of molecular dynamics and validated by comparing the theoretical predictions to experimental results. We characterize the distribution of peak forces and on correlations with the system size and with the structure classification as characterized by the CATH scheme. We identify proteins with the biggest forces and show that they belong to few topology classes. We determine which protein segments act as mechanical clamps and show that, in most cases, they correspond to long stretches of parallel beta-strands, but other mechanisms are also possible. We then consider stretching by fluid flows. We show that unfolding induced by a uniform flow shows a richer behavior than that in the force clamp. The dynamics of unfolding is found to depend strongly on the selection of the amino acid, usually one of the termini, which is anchored. These features offer potentially wider diagnostic tools to investigate structure of proteins compared to experiments based on the atomic force microscopy. [Preview Abstract] |
Session T21: DCOMP Business Meeting
Sponsoring Units: DCOMPChair: Ann Chaka, National Institute of Standards and Technology
Room: Colorado Convention Center 106
Wednesday, March 7, 2007 5:45PM - 6:45PM |
T21.00001: DCOMP Business Meeting |
Session T1: Congress: Change in Control! Change for Science?
Chair: Michael S. Lubell, American Physical Society and City College of New YorkRoom: Adam's Mark Hotel Plaza Ballroom ABC
Wednesday, March 7, 2007 7:30PM - 9:00PM |
T1.00001: Congress: Change in Control! Change for Science? Moderator: Michael S. Lubell, American Physical Society and The City College of CUNY\newline Panelists: Current and former Hill Staffers \newline \newline The November 2006 election put the Democrats in control of both house of Congress for the first time in twelve years. The panel of experts will use their wisdom and predictive powers to assess the impact of the political change on science policy and science budgets. Two former Hill staffers will provide the view from the outside; two current staffers will provide the enlightenment from the inside. [Preview Abstract] |
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