liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
The effect of glycosylation on the structure of designed four-helix bundle motifs
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology.
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology.
2000 (English)In: JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2, ISSN 0300-9580, no 3, 459-464 p.Article in journal (Refereed) Published
Abstract [en]

A galactose-, 1, and a cellobiose derivative, 2, have been site selectively, post-translationally, incorporated into a folded helix-loop-helix dimer LA-42b in a one step reaction at room temperature. The structural effects on the folded peptide upon glycosylation have been studied by CD and NMR spectroscopy. The negative value of the mean residue ellipticity of the folded peptide, LA-42b, was raised from -19000 +/- 1000 to -21200 +/- 1000 deg cm(2) dmol(-1) upon introduction of the galactose derivative and to -19500 +/- 1000 deg cm(2) dmol(-1) upon introduction of the cellobiose derivative, showing that the helical content was increased. The dissociation constant of the dimer decreased from 120 to 30 mu M upon glycosylation. The introduction of 1 into GTD-C, a folded helix-loop-helix dimer with a well defined tertiary structure, had little structural impact. Glycosylation stabilises the folded structure of proteins with partially exposed hydrophobic cores but has little effect on well-packed proteins.

Place, publisher, year, edition, pages
2000. no 3, 459-464 p.
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-49836OAI: oai:DiVA.org:liu-49836DiVA: diva2:270732
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2011-01-14

Open Access in DiVA

No full text

Authority records BETA

Dolphin, GunnarBaltzer, Lars

Search in DiVA

By author/editor
Dolphin, GunnarBaltzer, Lars
By organisation
The Institute of TechnologyDepartment of Physics, Chemistry and Biology
Engineering and Technology

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 37 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf