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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

Buijs, Jos; Ramstrom, Margareta; Danfelter, Mikael LU ; Larsericsdotter, Helen; Hakansson, Per and Oscarsson, Sven (2003) In Journal of Colloid and Interface Science 263(2). p.441-448
Abstract
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... (More)
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). (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Colloid and Interface Science
volume
263
issue
2
pages
441 - 448
publisher
Elsevier
external identifiers
  • pmid:12909033
  • scopus:0038723387
ISSN
1095-7103
DOI
language
English
LU publication?
yes
id
1799e9c2-321d-4a58-97d0-11b226e45eb0 (old id 1127240)
date added to LUP
2008-06-02 14:31:13
date last changed
2018-05-29 10:27:44
@article{1799e9c2-321d-4a58-97d0-11b226e45eb0,
  abstract     = {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).},
  author       = {Buijs, Jos and Ramstrom, Margareta and Danfelter, Mikael and Larsericsdotter, Helen and Hakansson, Per and Oscarsson, Sven},
  issn         = {1095-7103},
  language     = {eng},
  number       = {2},
  pages        = {441--448},
  publisher    = {Elsevier},
  series       = {Journal of Colloid and Interface Science},
  title        = {Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry},
  url          = {http://dx.doi.org/},
  volume       = {263},
  year         = {2003},
}