his.sePublikasjoner
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Surface interactions in the complex between cytochrome f and the E43Q/D44N and E59K/E60Q plastocyanin double mutants as determined by (1)H-NMR chemical shift analysis
Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden / Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, USA.
Högskolan i Skövde, Institutionen för naturvetenskap. Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.ORCID-id: 0000-0002-3053-4543
Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, The Netherlands.
Department of Molecular Biotechnology, Chalmers University of Technology, Göteborg, Sweden.
2001 (engelsk)Inngår i: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 10, nr 12, s. 2623-2626Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

A combination of site-directed mutagenesis and NMR chemical shift perturbation analysis of backbone and side-chain protons has been used to characterize the transient complex of the photosynthetic redox proteins plastocyanin and cytochrome f. To elucidate the importance of charged residues on complex formation, the complex of cytochrome f and E43Q/D44N or E59K/E60Q spinach plastocyanin double mutants was studied by full analysis of the (1)H chemical shifts by use of two-dimensional homonuclear NMR spectra. Both mutants show a significant overall decrease in chemical shift perturbations compared with wild-type plastocyanin, in agreement with a large decrease in binding affinity. Qualitatively, the E43Q/D44N mutant showed a similar interaction surface as wild-type plastocyanin. The interaction surface in the E59K/E60Q mutant was distinctly different from wild type. It is concluded that all four charged residues contribute to the affinity and that residues E59 and E60 have an additional role in fine tuning the orientation of the proteins in the complex.

sted, utgiver, år, opplag, sider
John Wiley & Sons, 2001. Vol. 10, nr 12, s. 2623-2626
HSV kategori
Forskningsprogram
Naturvetenskap
Identifikatorer
URN: urn:nbn:se:his:diva-9896DOI: 10.1110/ps.27101ISI: 000172416600023PubMedID: 11714931Scopus ID: 2-s2.0-0035177819OAI: oai:DiVA.org:his-9896DiVA, id: diva2:743799
Tilgjengelig fra: 2014-09-05 Laget: 2014-09-05 Sist oppdatert: 2017-12-05bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstPubMedScopus

Personposter BETA

Ejdebäck, Mikael

Søk i DiVA

Av forfatter/redaktør
Ejdebäck, Mikael
Av organisasjonen
I samme tidsskrift
Protein Science

Søk utenfor DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 1474 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf