SwePub
Sök i LIBRIS databas

  Extended search

onr:"swepub:oai:lup.lub.lu.se:30b0b20a-0bee-4f41-b117-fc822bfb98d9"
 

Search: onr:"swepub:oai:lup.lub.lu.se:30b0b20a-0bee-4f41-b117-fc822bfb98d9" > Determination of th...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist
  • Sgourakis, Nikolaos G. (author)

Determination of the Structures of Symmetric Protein Oligomers from NMR Chemical Shifts and Residual Dipolar Couplings

  • Article/chapterEnglish2011

Publisher, publication year, extent ...

  • 2011-04-05
  • American Chemical Society (ACS),2011

Numbers

  • LIBRIS-ID:oai:lup.lub.lu.se:30b0b20a-0bee-4f41-b117-fc822bfb98d9
  • https://lup.lub.lu.se/record/2094011URI
  • https://doi.org/10.1021/ja111318mDOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • Symmetric protein dimers, trimers, and higher-order cyclic oligomers play key roles in many biological processes. However, structural studies of oligomeric systems by solution NMR can be difficult due to slow tumbling of the system and the difficulty in identifying NOE interactions across protein interfaces. Here, we present an automated method (RosettaOligomers) for determining the solution structures of oligomeric systems using only chemical shifts, sparse NOEs, and domain orientation restraints from residual dipolar couplings (RDCs) without a need for a previously determined structure of the monomeric subunit. The method integrates previously developed Rosetta protocols for solving the structures of monomeric proteins using sparse NMR data and for predicting the structures of both nonintertwined and intertwined symmetric oligomers. We illustrated the performance of the method using a benchmark set of nine protein dimers, one trimer, and one tetramer with available experimental data and various interface topologies. The final converged structures are found to be in good agreement with both experimental data and previously published high-resolution structures. The new approach is more readily applicable to large oligomeric systems than conventional structure-determination protocols, which often require a large number of NOEs, and will likely become increasingly relevant as more high-molecular weight systems are studied by NMR

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Lange, Oliver F. (author)
  • DiMaio, Frank (author)
  • André, IngemarLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fkm2-ian (author)
  • Fitzkee, Nicholas C. (author)
  • Rossi, Paolo (author)
  • Montelione, Gaetano T. (author)
  • Bax, Ad (author)
  • Baker, David (author)
  • Biokemi och StrukturbiologiCentrum för Molekylär Proteinvetenskap (creator_code:org_t)

Related titles

  • In:Journal of the American Chemical Society: American Chemical Society (ACS)133:16, s. 6288-62981520-51260002-7863

Internet link

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Search outside SwePub

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view