Towards the structural characterization of intrinsically disordered proteins by saxs and MD simulation

Tomotaka Oroguchi, Mitsunori Ikeguchi, Mamoru Sato

Research output: Contribution to journalArticle

8 Citations (Scopus)


Dynamical structures of intrinsically disordered proteins (IDPs) and multi-domain proteins that include large ID regions between the domains are unable to be determined by such conventional methods as X-ray crystallography and electron microscopy. Small-angle X-ray scattering (SAXS) is suitable to determine low-resolution structures of proteins and protein complexes in solution, but the structural data on protein dynamics are averaged over the structural ensemble in protein solution. To overcome this problem, we have developed a novel method, named MD-SAXS, of the combined use of SAXS and molecular dynamics (MD) simulation to analyze protein dynamics in solution of multi-subunit protein complexes and multi-domain proteins toward the structural characterization of IDPs. Here we show validity of the method through the structural characterization of restriction Endonuclease EcoO109I.

Original languageEnglish
Article number012005
JournalJournal of Physics: Conference Series
Issue number1
Publication statusPublished - 2011 Jan 1
Externally publishedYes


ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this