uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
A hydrodynamic comparison of solution and gas phase proteins and their complexes.
Show others and affiliations
2014 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 118, no 29Article in journal (Refereed) Published
Abstract [en]

The extent to which protein structures are preserved on transfer from solution to gas phase is a central question for native mass spectrometry. Here we compare the collision cross sections (Ω) of a wide range of different proteins and protein complexes (15-500 kDa) with their corresponding Stokes radii (RS). Using these methods, we find that Ω and RS are well correlated, implying overall preservation of protein structure in the gas phase. Accounting for protein hydration, a scaling term is required to bring Ω and RS into parity. Interestingly, the magnitude of this scaling term agrees almost entirely with the drag factor proposed by Millikan. RS were then compared with various different predicted values of Ω taken from their atomic coordinates. We find that many of the approaches used to obtained Ω from atomic coordinates miscalculate the physical sizes of the proteins in solution by as much as 20%. Rescaling of Ω estimated from atomic coordinates may therefore seem appropriate as a general method to bring theoretical values in line with those observed in solution.

Place, publisher, year, edition, pages
2014. Vol. 118, no 29
National Category
Analytical Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-302810DOI: 10.1021/jp501950dPubMedID: 24945444OAI: oai:DiVA.org:uu-302810DiVA: diva2:967748
Available from: 2016-09-09 Created: 2016-09-09 Last updated: 2016-09-09

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Marklund, Erik
In the same journal
Journal of Physical Chemistry B
Analytical Chemistry

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

ReferencesLink to record
Permanent link

Direct link