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Weak and Transient Protein Interactions Determined by Solid-State NMR

Journal Article


Abstract


  • Despite their roles in controlling many cellular

    processes, weak and transient interactions between large

    structured macromolecules and disordered protein segments

    cannot currently be characterized at atomic resolution by Xray

    crystallography or solution NMR. Solid-state NMR does

    not suffer from the molecular size limitations affecting solution

    NMR, and it can be applied to molecules in different

    aggregation states, including non-crystalline precipitates and

    sediments. A solid-state NMR approach based on high

    magnetic fields, fast magic-angle sample spinning, and deuteration

    provides chemical-shift and relaxation mapping that

    enabled the characterization of the structure and dynamics of

    the transient association between two regions in an 80 kDa

    protein assembly. This led to direct verification ofamechanism

    of regulation of E. coli DNA metabolism

Authors


  •   Dannatt, Hugh R W. (external author)
  •   Felletti, Michelle (external author)
  •   Jehle, S (external author)
  •   Wang, Yao (external author)
  •   Emsley, Lyndon (external author)
  •   Dixon, Nicholas E.
  •   Lesage, A S. (external author)
  •   Pintacuda, Guido (external author)

Publication Date


  • 2016

Citation


  • Dannatt, H. R W., Felletti, M., Jehle, S., Wang, Y., Emsley, L., Dixon, N. E., Lesage, A. & Pintacuda, G. (2016). Weak and Transient Protein Interactions Determined by Solid-State NMR. Angewandte Chemie International Edition, 55 6638-6641.

Scopus Eid


  • 2-s2.0-84964355473

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/4691

Number Of Pages


  • 3

Start Page


  • 6638

End Page


  • 6641

Volume


  • 55

Abstract


  • Despite their roles in controlling many cellular

    processes, weak and transient interactions between large

    structured macromolecules and disordered protein segments

    cannot currently be characterized at atomic resolution by Xray

    crystallography or solution NMR. Solid-state NMR does

    not suffer from the molecular size limitations affecting solution

    NMR, and it can be applied to molecules in different

    aggregation states, including non-crystalline precipitates and

    sediments. A solid-state NMR approach based on high

    magnetic fields, fast magic-angle sample spinning, and deuteration

    provides chemical-shift and relaxation mapping that

    enabled the characterization of the structure and dynamics of

    the transient association between two regions in an 80 kDa

    protein assembly. This led to direct verification ofamechanism

    of regulation of E. coli DNA metabolism

Authors


  •   Dannatt, Hugh R W. (external author)
  •   Felletti, Michelle (external author)
  •   Jehle, S (external author)
  •   Wang, Yao (external author)
  •   Emsley, Lyndon (external author)
  •   Dixon, Nicholas E.
  •   Lesage, A S. (external author)
  •   Pintacuda, Guido (external author)

Publication Date


  • 2016

Citation


  • Dannatt, H. R W., Felletti, M., Jehle, S., Wang, Y., Emsley, L., Dixon, N. E., Lesage, A. & Pintacuda, G. (2016). Weak and Transient Protein Interactions Determined by Solid-State NMR. Angewandte Chemie International Edition, 55 6638-6641.

Scopus Eid


  • 2-s2.0-84964355473

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/4691

Number Of Pages


  • 3

Start Page


  • 6638

End Page


  • 6641

Volume


  • 55