mdh.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • 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
Thermodynamic analysis of lysozyme adsorbed to silica
Mälardalen University, Department of Biology and Chemical Engineering.
Mälardalen University, Department of Biology and Chemical Engineering.
Mälardalen University, Department of Biology and Chemical Engineering. Uppsala University, Sweden.
2004 (English)In: Journal of colloid and interface science, ISSN 0021-9797, Vol. 276, no 2, 261-268 p.Article in journal (Refereed) Published
Abstract [en]

The structural stability of hen egg white lysozyme in solution and adsorbed to small colloidal silica particles at various surface concentrations was investigated using hydrogen-deuterium (H/D) exchange in combination with mass spectrometry (HDX-MS) and differential scanning calorimetry (DSC). The combination of HDX-MS and DSC allows a full thermodynamic analysis of the lysozyme structure as both the enthalpy and the Gibbs free energy can be derived from the various measurements. Moreover, both HDX-MS and DSC provide information on the relative structural heterogeneity of lysozyme in the adsorbed state compared to that in solution. Results demonstrated that at high surface coverage, the structural stability of lysozyme was only marginally affected by adsorption to silica particles whereas the unfolding enthalpy decreased by more than 10%, meaning that the entropy of lysozyme increased with a similar value upon adsorption. Furthermore, the structural heterogeneity increased considerably. At lower surface concentrations, the structural heterogeneity increased further whereas the enthalpy of unfolding decreased. Further analyses of the HDX-MS experiments clearly indicated that folding/unfolding of lysozyme occurs through a two-domain process. These two domains had a similar amount of structural elements and a difference in stabilization energy of 8 kJ/mol, regardless if lysozyme was in solution or adsorbed to silica.

Place, publisher, year, edition, pages
2004. Vol. 276, no 2, 261-268 p.
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:mdh:diva-1941DOI: 10.1016/j.jcis.2004.03.056ISI: 000223006200001PubMedID: 15271551Scopus ID: 2-s2.0-3242723297OAI: oai:DiVA.org:mdh-1941DiVA: diva2:114604
Available from: 2006-03-09 Created: 2006-03-09 Last updated: 2015-07-07Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedScopus

Search in DiVA

By author/editor
Oscarsson, Sven
By organisation
Department of Biology and Chemical Engineering
Physical Chemistry

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 59 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • 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