Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1127240
- author
- Buijs, Jos ; Ramstrom, Margareta ; Danfelter, Mikael LU ; Larsericsdotter, Helen ; Hakansson, Per and Oscarsson, Sven
- organization
- publishing date
- 2003
- 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
- 10.1016/S0021-9797(03)00401-6
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151)
- id
- 1799e9c2-321d-4a58-97d0-11b226e45eb0 (old id 1127240)
- date added to LUP
- 2016-04-01 12:22:17
- date last changed
- 2022-04-21 06:32:25
@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/10.1016/S0021-9797(03)00401-6}},
doi = {{10.1016/S0021-9797(03)00401-6}},
volume = {{263}},
year = {{2003}},
}