Intrinsic dynamics of proteins and regulation of allosteric communication

PHYS 134

Chakra Chennubhotla, chakra@ccbb.pitt.edu1, Zheng Yang2, and Ivet Bahar, bahar@pitt.edu2. (1) Department of Computational Biology, School of Medicine, University of Pittsburgh, 3064 BST3, 3501 Fifth Ave, Pittsburgh, PA 15213, (2) Department of Computational Biology, School of Medicine, University of Pittsburgh, 3064 BST3, 3501 Fifth Ave, Pittsburgh, PA 15213
An emerging concept, supported by both theory and experiments, is intrinsic ability of proteins to sample functional changes in structure. Because such motions are insensitive to structural details, elastic network models have been broadly used in recent years toward efficiently elucidating such allosteric responses. Another recent application of network models has been the modeling of inter-residue interactions as a Markovian stochastic process, using information theory and spectral graph methods. Recent studies are now elucidating the connection between the physically motivated studies based on elastic network models, and those based on information theory and methods. Application to GroEL-GroES will be presented, where the low frequency mode of motion will be shown to directly affect the interaction between residues that act as ‘messengers' that transmit allosteric signals. Disruption of signals by conformational changes undergone during the global modes of motions emerges as a mechanism of regulating allosteric communication.
 

Multiscale Modeling in Biophysics
8:20 AM-12:20 PM, Monday, April 7, 2008 Morial Convention Center -- Rm. R03, Oral

Division of Physical Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008