This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. During the past five years there has been a tremendous growth of the number of virus structures solved by X-ray crystallography and cryo electron microscopy (EM) experiments, including virus capsids adopting several functionally relevant conformations. In addition, with time resolved small angle scattering experiments dynamics of viruses can now be monitored and for some systems several intermediate have been observed. These large-scale rearrangements are an integral part of the life cycle of the virus and have been observed in the maturation process, during assembly and may be involved in the release of RNA during infection. Disrupting the assembly or the maturation processes in viruses may be potential targets for antiviral activities. Thus, the description, prediction and exploration of such conformational changes for viruses are essential to understand their mechanism of activity and should be helpful in the development of new drugs.
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Arthur, Evan J; King, John T; Kubarych, Kevin J et al. (2014) Heterogeneous preferential solvation of water and trifluoroethanol in homologous lysozymes. J Phys Chem B 118:8118-27 |
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