Journal ArticleDOI
Probing conformational changes in proteins by mass spectrometry
TLDR
The authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.Abstract:
Mass spectrometry has found wide application for the elucidation of the primary structures of proteins. However, with the exception of topographical studies of membrane-bound proteins, mass spectrometry has not previously been utilized to obtain information concerning in three-dimensional conformation of proteins. In the present communication, the authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.read more
Citations
More filters
Journal ArticleDOI
Conformational stability of Syrian hamster prion protein PrP(90-231).
Megan Grabenauer,Thomas Wyttenbach,Narinder Sanghera,Susan E. Slade,Teresa J. T. Pinheiro,James H. Scrivens,Michael T. Bowers +6 more
TL;DR: Evidence is found for at least one very stable conformation of a truncated form of recombinant PrP(C) consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K.
Journal ArticleDOI
An electrospray ionization mass spectrometry investigation of 1-anilino-8-naphthalene-sulfonate (ANS) binding to proteins.
TL;DR: The binding of 1-anilino-8-naphthalene-sulfonic acid to various globular proteins at acidic pH has been investigated by electrospray ionization mass spectrometry (ESI-MS), suggesting heterogeneity of gas phase conformations.
Journal ArticleDOI
Calmodulin-peptide interactions: apocalmodulin binding to the myosin light chain kinase target-site.
Tessa J. Hill,Daniel Lafitte,James I. Wallace,Helen J. Cooper,Philip O. Tsvetkov,Peter J. Derrick +5 more
TL;DR: It is proposed that calcium binding to form the calmodulin-RS20-Ca(4) complex occurs after an initial RS20-calmodulin binding event, and serves to secure the target within the cal modulin structure.
Journal ArticleDOI
Modulation of E-Cadherin Monomer Folding by Cooperative Binding of Calcium Ions†
Olivier Courjean,Guillaume Chevreux,Emilie Perret,Anne Morel,Sarah Sanglier,Noelle Potier,Jürgen Engel,and Alain van Dorsselaer,Helene Feracci +8 more
TL;DR: It is demonstrated that E/EC12 binds three calcium ions, with an average KD of 20 +/- 0.7 microM, and the D103A mutation (a residue involved in E-cadherin adhesive function) modified calcium binding and led to a loss of cooperativity and the absence of structural changes, despite calcium binding.
Journal ArticleDOI
Conformations of gas-phase lysozyme ions produced from two different solution conformations.
TL;DR: Disulfide-intact gaseous lysozyme ions generated from the denatured state in water/methanol (2/8) refold into compact structures in the gas phase on a time scale of milliseconds or less.
Related Papers (5)
Electrospray ionization for mass spectrometry of large biomolecules
Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry
Viswanatham Katta,Brian T. Chait +1 more