conformational temperature-dependent behavior of a histone h2ax a coarse-grained monte carlo approach via knowledge-based interaction potentials组蛋白的构象与温度有关的行为h2ax粗粒度的蒙特卡罗方法通过基于知识的相互作用势.pdfVIP

Conformational Temperature-Dependent Behavior of a Histone H2AX: A Coarse-Grained Monte Carlo Approach Via Knowledge-Based Interaction Potentials 1 2 3 1,4,5 Miriam Fritsche *, Ras B. Pandey , Barry L. Farmer , Dieter W. Heermann 1 Institute for Theoretical Physics, University of Heidelberg, Heidelberg, Germany, 2 Department of Physics and Astronomy, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America, 3 Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright Patterson Air Force Base, Ohio, United States of America, 4 Institute for Molecular Biophysics, The Jackson Laboratory, Bar Harbor, Maine, United States of America, 5 Interdisciplinary Center for Scientific Computing, Heidelberg, Germany Abstract Histone proteins are not only important due to their vital role in cellular processes such as DNA compaction, replication and repair but also show intriguing structural properties that might be exploited for bioengineering purposes such as the development of nano-materials. Based on their biological and technological implications, it is interesting to investigate the structural properties of proteins as a function of temperature. In this work, we study the spatial response dynamics of the histone H2AX, consisting of 143 residues, by a coarse-grained bond fluctuating model for a broad range of normalized temperatures. A knowledge-based interaction matrix is used as input for the residue-residue Lennard-Jones potential. We find a variety of equilibrium structures including global globular configurations at low normalized temperature (T ~0:014), combination of segmental globules and elongated chains (T ~0:016,0:017), predominantly elongated chains (T ~0:019,0:020), as well as univers