Assembly of Matrix Protein VP40 of Ebola Virus by Hydrogen-Deuterium Exchange Mass Spectrometry

摘要

The transitional state study data suggested a subtle trend reflecting a diffuse conformational response at mid-level denaturing concentration. However, the peptide data did not provide sufficient resolution to confirm a localized sequential destabilization. The octameric state study confirmed the model of Gomis-Ruth et al, which indicates that only the N-domain is involved in assembly, in an anti-parallel fashion. The N-domain plays a significant role in the stabilization of the C-domain and N-tail. Upon octamerization, the sequestering of the N-domain causes these regions to become unstructured. The HDX data and Haddock software will be used in the near future to develop an octameric model, including the location of the N-tail and the entire C-domain, which have not previously been reported.