Probing the Hydrophobic Effect of Noncovalent Complexes by Mass Spectrometry

Metadata Label Value
Author(s) Bich, Claudia, Baer, Samuel, Jecklin, Matthias C., Zenobi, Renato
Publication Type Journal Items, Publication Status: Published
Full Text Search SFX for a Full-Text version of this document
Import to Mendeley

Detailed Information

Metadata Field Content
Title Probing the Hydrophobic Effect of Noncovalent Complexes by Mass Spectrometry
Author(s) Bich, Claudia
Baer, Samuel
Jecklin, Matthias C.
Zenobi, Renato
Journal or Series Title Journal of the American Society for Mass Spectrometry
Volume Number 21
Issue Number 2
Start Page 286
End Page 289
ISSN 1044-0305
Publisher Elsevier Science
Publication Place New York
Publication Date 2010
Abstract The study of noncovalent interactions by mass spectrometry has become an active field of research in recent years. The role of the different noncovalent intermolecular forces is not yet fully understood since they tend to be modulated upon transfer into the gas phase. The hydrophobic effect, which plays a major role in protein folding, adhesion of lipid bilayers, etc., is absent in the gas phase. Here, noncovalent complexes with different types of interaction forces were investigated by mass spectrometry and compared with the complex present in solution. Creatine kinase (CK), glutathione S-transferase (GST), ribonuclease S (RNase S), and leucine zipper (LZ), which have dissociation constants in the nM range, were studied by native nanoelectrospray mass spectrometry (nanoESI-MS) and matrix-assisted laser desorption/ionization mash spectrometry (MALDI-MS) combined with chemical cross-linking (XL). Complexes interacting with hydrogen bonds survived the transfer into gas phase intact and were observed by nanoESI-MS. Complexes that are bound largely by the hydrophobic effect in solution were not detected or only at very low intensity. Complexes with mixed polar and hydrophobic interactions were detected by nanoESI-MS, most likely due to the contribution from polar interactions. All noncovalent complexes could easily be studied by XL MALDI-MS, which demonstrates that the noncovalently bound complexes are conserved, and a real "snap-shot" of the situation in solution can be obtained.
DOI 10.1016/j.jasms.2009.10.012
Additional Notes Received 29 August 2009, Revised 15 October 2009, Accepted 15 October 2009, Available online 28 October 2009
Document Type Article
Publication Status Published
Language English
Assigned Organisational Unit(s) 03430
Organisational Unit(s)
NEBIS System Number 000541631
Source Database ID WOS-000275344100012
Description File Name MIME Type Size
No details could be found
There are no links available for this record.
This record has not been viewed during this period

  author = "Bich, Claudia and Baer, Samuel and Jecklin, Matthias C. and Zenobi, Renato",
  title = "{P}robing the {H}ydrophobic {E}ffect of {N}oncovalent {C}omplexes by {M}ass {S}pectrometry",
  journal = "Journal of the American Society for Mass Spectrometry",
  year = 2010,
  volume = "21",
  number = "2",
  pages = "286--289",

E-Citations record created: Tue, 13 Apr 2010, 11:16:02 CET