Correction of Both NBD1 Energetics and Domain Interface Is Required to Restore ΔF508 CFTR Folding and Function
- W. Rabeh, F. Bossard, G. Lukács
- 20 January 2012
Hydrogen exchange mass spectrometry for studying protein structure and dynamics.
- L. Konermann, Jingxi Pan, Yu-Hong Liu
- BiologyChemical Society Reviews
- 22 February 2011
This tutorial review briefly discusses basic fundamentals of HDX/MS, before highlighting a number of recent developments and applications that facilitate the applicability of HDx/MS to membrane proteins, and to the characterization of short-lived protein folding intermediates.
Unraveling the mechanism of electrospray ionization.
- L. Konermann, E. Ahadi, A. Rodriguez, S. Vahidi
- ChemistryAnalytical Chemistry
- 2 January 2013
Electrospray ionization generates intact gas-phase ions from analytes in solution for mass spectrometric investigations and has been proposed for disordered polymers.
Acid-induced unfolding of cytochrome c at different methanol concentrations: electrospray ionization mass spectrometry specifically monitors changes in the tertiary structure.
- L. Konermann, D. J. Douglas
- 7 October 1997
The observed transition from low to high charge states is due to the breakdown of the tertiary structure in both cases, suggesting that ESI MS might be a general method to selectively monitor changes in the secondary structure of proteins.
Analysis of the absorption spectrum of photosystem II reaction centers: temperature dependence, pigment assignment, and inhomogeneous broadening.
- L. Konermann, A. Holzwarth
- 23 January 1996
The results suggest that the Chl content of the samples has been underestimated in many spectroscopic studies on the PSII-RC, based on theoretical calculations of the line shapes of the inhomogeneously broadened pigment spectra.
Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments
Recommendations arising from community discussions emerging out of the first International Conference on Hydrogen-Exchange Mass Spectrometry (IC-HDX; 2017) are provided, meant to represent both a consensus viewpoint and an opportunity to stimulate further additions and refinements as the field advances.
Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches.
- L. Konermann, X. Tong, Yan Pan
- Chemistry, BiologyJournal of Mass Spectrometry
- 1 August 2008
A simple method for the computational simulation of protein HDX patterns is described, a tool that can be helpful for the interpretation of isotope exchange data recorded under mixed EX1/EX2 conditions, and important aspects of .OH labeling include a striking dependence on protein concentration, and the tendency of commonly used solvent additives to act as highly effective radical scavengers.
A capillary mixer with adjustable reaction chamber volume for millisecond time-resolved studies by electrospray mass spectrometry.
- Derek J. Wilson, L. Konermann
- ChemistryAnalytical Chemistry
- 11 October 2003
Studies on the demetalation kinetics of chlorophyll reveal that the apparatus can reliably measure rate constants up to at least 100 s-1, which represents a substantial improvement over previous ESI-MS-based kinetic methods.
Symmetric Behavior of Hemoglobin α- and β- Subunits during Acid-Induced Denaturation Observed by Electrospray Mass Spectrometry†
- B. Boys, Mark C. Kuprowski, L. Konermann
- Chemistry, Biology
- 24 August 2007
It is concluded that the acid-induced denaturation of Hb follows a highly symmetric mechanism and heme-deficient dimers are virtually undetectable for the freshly prepared Hb derivatives studied herein at any pH.
Hydrogen/deuterium exchange mass spectrometry with top-down electron capture dissociation for characterizing structural transitions of a 17 kDa protein.
- Jingxi Pan, Jun Han, C. Borchers, L. Konermann
- Biology, ChemistryJournal of the American Chemical Society
- 11 August 2009
The findings demonstrate that the level of structural information obtainable with top-down ECD for small to medium-sized proteins considerably surpasses that of traditional HDX-MS experiments, while at the same time greatly reducing undesired amide back exchange.