scholarly journals Theory of the protein equilibrium population snapshot by H/D exchange electrospray ionization mass spectrometry (PEPS-HDX-ESI-MS) method used to obtain protein folding energies/rates and selected supporting experimental evidence

2012 ◽  
Vol 330-332 ◽  
pp. 63-70 ◽  
Author(s):  
Rohana Liyanage ◽  
Nagarjuna Devarapalli ◽  
Derek B. Pyland ◽  
Latisha M. Puckett ◽  
N.H. Phan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Folding ◽  
Experimental Evidence ◽  
Electrospray Ionization ◽  
Electrospray Ionization Mass Spectrometry ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Esi Ms

scholarly journals Analysis of Protein Folding Equilibria by Nano-Electrospray-Ionization Mass Spectrometry

2002 ◽  
Vol 16 (3-4) ◽  
pp. 361-370 ◽  
Author(s):  
Irena Matecko ◽  
Norbert Müller ◽  
Rita Grandori
Keyword(s):  
Mass Spectrometry ◽  
Protein Folding ◽  
Electrospray Ionization ◽  
Electrospray Ionization Mass Spectrometry ◽  
Tertiary Structure ◽  
Molten Globule ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Conformational States ◽  
Esi Ms

This paper summarizes recent findings from our group concerning applications of electrospray-ionization mass spectrometry (ESI-MS) to the study of protein folding. Nano-ESI-MS was employed for the investigation of protein conformational states under varying solvent conditions and at varying values of the instrumental parameters. The effect of trifluoroethanol (TFE) on a peptide and acid-unfolded cytochromec(cytc), monitored by circular dichroism (CD) and time-of-flight ESI-MS, illustrates the specificity of the latter technique for features of protein tertiary structure. Measurements on marginally stable protein states indicate that it is possible to identify operational conditions for nano-ESI-MS in which none of the instrumental parameters limits conformational stability in the protein sample. Results described here show that changes in the charge-state distributions (CSDs) under controlled conditions allow not only discriminating between native and denatured states, but also monitoring minor conformational changes, like the transition from molten globule to native state. These studies underscore the potential of mass spectrometry methods for the analysis of heterogeneous samples and, in particular, for the characterization of dynamic equilibria involving different conformational states.

scholarly journals Analysis of Inositol Phosphate Metabolism by Capillary Electrophoresis Electrospray Ionization Mass Spectrometry (CE-ESI-MS)

2020 ◽  
Author(s):  
Danye Qiu ◽  
Miranda S. Wilson ◽  
Verena B. Eisenbeis ◽  
Robert K. Harmel ◽  
Esther Riemer ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
Electrospray Ionization ◽  
Electrospray Ionization Mass Spectrometry ◽  
Inositol Phosphate ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Phosphate Metabolism ◽  
Esi Ms ◽  
Inositol Phosphate Metabolism

AbstractThe analysis of myo-inositol phosphates (InsPs) and myo-inositol pyrophosphates (PP-InsPs) is a daunting challenge due to the large number of possible isomers, the absence of a chromophore, the high charge density, the low abundance, and the instability of the esters and anhydrides. Given their importance in biology, an analytical approach to follow and understand this complex signaling hub is highly desirable. Here, capillary electrophoresis (CE) coupled to electrospray ionization mass spectrometry (ESI-MS) is implemented to analyze complex mixtures of InsPs and PP-InsPs with high sensitivity. Stable isotope labeled (SIL) internal standards allow for matrix-independent quantitative assignment. The method is validated in wild-type and knockout mammalian cell lines and in model organisms. SIL-CE-ESI-MS enables for the first time the accurate monitoring of InsPs and PP-InsPs arising from compartmentalized cellular synthesis pathways, by feeding cells with either [13C6]-myo-inositol or [13C6]-D-glucose. In doing so, we uncover that there must be unknown inositol synthesis pathways in mammals, highlighting the unique potential of this method to dissect inositol phosphate metabolism and signalling.

Developments in Electrospray Ionization Mass Spectrometry of Non-Covalent DNA–Ligand Complexes

2011 ◽  
Vol 64 (6) ◽  
pp. 705 ◽  
Author(s):  
Jennifer L. Beck
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Ionization ◽  
Electrospray Ionization Mass Spectrometry ◽  
Short Review ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Quadruplex Dna ◽  
Esi Ms ◽  
Selective Ligands ◽  
Ligand Interactions

Many anti-cancer drugs function by binding non-covalently to double-stranded (ds) DNA. Electrospray ionization mass spectrometry (ESI-MS) has emerged over the past decade as a sensitive technique for the determination of stoichiometries and relative binding affinities of DNA–ligand interactions. The chromosome contains nucleotide sequences, for example, guanosine-rich regions, that predispose them to the formation of higher order structures such as quadruplex DNA (qDNA). Sequences that form qDNA are found in the telomeres. The proposal that ligands that stabilize qDNA might interfere with the activity of telomerase in cancer cells has stimulated the search for ligands that are selective for qDNA over dsDNA. The insights gained from the development of ESI-MS methods for analysis of non-covalent dsDNA–ligand complexes are now being applied in the search for qDNA-selective ligands. ESI-MS is a useful first-pass screening technique for qDNA-binding ligands. This short review describes some experimental considerations for ESI-MS analysis of DNA–ligand complexes, briefly addresses the question of whether non-covalent DNA–ligand complexes are faithfully transferred from solution to the gas phase, discusses ion mobility mass spectrometry as a technique for probing this issue, and highlights some recent ESI-MS studies of qDNA-selective ligands.

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