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Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry
Uppsala University, Sweden.
Uppsala University, Sweden.
Uppsala University, Sweden.
Mälardalen University, Department of Biology and Chemical Engineering.
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2003 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, Vol. 263, no 2, 441-448 p.Article in journal (Refereed) Published
Abstract [en]

A new method is presented for monitoring the conformational stability of various parts of a protein that is physically adsorbed onto nanometer-sized silica particles. The method employs hydrogen/deuterium (H/D) exchange of amide hydrogens, a process that is extremely sensitive to structural features of proteins. The resulting mass increase is analyzed with Fourier transform ion cyclotron resonance (FTICR) mass spectrometry. Higher structural specificity is obtained by enzymatically cleaving the adsorbed proteins prior to mass spectrometric analysis. The mass increases of four peptic fragments of myoglobin are followed as a function of the H/D exchange time. The four peptic fragments cover 90% of the myoglobin structure. Two of the peptic fragments, located in the middle of the myoglobin sequence and close to the heme group, do not show any adsorption-induced changes in their structural stability, whereas the more stable C- and N-terminal fragments are destabilized. Interestingly, for the N-terminal fragment, comprising residues 1–29, two distinct and equally large conformational populations are observed. One of these populations has a stability similar to that in solution (−23 kJ/mol), whereas the other population is highly destabilized upon adsorption (−11 kJ/mol).

Place, publisher, year, edition, pages
2003. Vol. 263, no 2, 441-448 p.
Keyword [en]
Adsorption, Conformation, HD exchange, Mass spectrometry, Myoglobin, Protein, Stability, Structure
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:mdh:diva-2562DOI: 10.1016/S0021-9797(03)00401-6ISI: 000183927000012Scopus ID: 2-s2.0-0038723387OAI: oai:DiVA.org:mdh-2562DiVA: diva2:115225
Available from: 2006-03-09 Created: 2006-03-09 Last updated: 2015-07-06Bibliographically approved

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CiteExportLink to record
Permanent link

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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
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Output format
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  • asciidoc
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