Mobile Protons Limit the Stability of Salt Bridges in the Gas Phase: Implications for the Structures of Electrosprayed Protein Ions

2021 ◽  
Vol 125 (15) ◽  
pp. 3803-3814
Author(s):  
Lars Konermann ◽  
Elnaz Aliyari ◽  
Justin H. Lee
Keyword(s):  
Gas Phase ◽  
Salt Bridges ◽  
Protein Ions ◽  
The Stability

Probing the Stability and Structure of Metalloporphyrin Complexes with Basic Peptides by Mass Spectrometry

2005 ◽  
Vol 11 (1) ◽  
pp. 65-72 ◽  
Author(s):  
Emily E. Jellen ◽  
Victor Ryzhov
Keyword(s):  
Gas Phase ◽  
Metal Ion ◽  
Basic Amino Acid ◽  
Quadrupole Ion Trap ◽  
Model Systems ◽  
Central Metal ◽  
Salt Bridges ◽  
Charge Solvation ◽  
The Stability ◽  
Basic Peptides

The stability and structure of non-covalent complexes of various peptides contatining basic amino acid residues (Arg, Lys) with metalloporphyrins were studied in a quadrupole ion trap mass spectrometer. The complexes of heme and three other metalloporphyrins with a variety of basic peptides and model systems were formed via electrospray ionization (ESI) and their stability was probed by energy-variable collision-induced dissociation (CID). A linear dependence for basic peptides and model compounds/metalloporphyrin complexes was observed in the plots of stability versus degrees of freedom and was used to evaluate relative bond strength. These results were then compared with previous data obtained for complexes of metalloporphyrins with His-containing peptides and peptides containing no basic amino acids. The binding strengths of Lys-containing peptide complexes in the gas phase was found to be almost as strong as that of Arg-containing complexes. Both systems showed stronger binding than His-containing peptides studied previously. To probe the structure of Arg and Lys non-covalent complexes (charge solvation versus salt bridges), two techniques, CID and ion–molecule reactions, were used. CID experiments indicate that the gas-phase complexes are most likely formed by charge solvation of the central metal ion in the metalloporphyrin by basic side chains of Arg or Lys. Results from the ion–molecule reaction studies are consistent with the charge solvation structure as well.

Importance of Two Buried Salt Bridges in the Stability and Folding Pathway of Barnase†

Biochemistry ◽  
1996 ◽  
Vol 35 (21) ◽  
pp. 6786-6794 ◽  
Author(s):  
A. C. Tissot ◽  
S. Vuilleumier ◽  
A. R. Fersht
Keyword(s):  
Folding Pathway ◽  
Salt Bridges ◽  
The Stability

Visible and ultraviolet spectroscopy of gas phase protein ions

2011 ◽  
Vol 13 (37) ◽  
pp. 16494 ◽  
Author(s):  
Rodolphe Antoine ◽  
Philippe Dugourd
Keyword(s):  
Gas Phase ◽  
Ultraviolet Spectroscopy ◽  
Protein Ions ◽  
Phase Protein

Two- and four-armed hetero porphyrin dimers: Influence of the number of arms on the stability and specific recognition behaviour

2021 ◽  
Author(s):  
Masaki Ueda ◽  
Masaki Kimura ◽  
Shinobu Miyagawa ◽  
Masaya Naito ◽  
Hikaru Takaya ◽  
...  
Keyword(s):  
Salt Bridges ◽  
Specific Recognition ◽  
Self Assembled ◽  
The Stability ◽  
Porphyrin Dimers

In this study we self-assembled the four-armed porphyrin hetero dimer capsule Cap4, stabilized through amidinium–carboxylate salt bridges, in CH2Cl2 and CHCl3. The dimer capsule Cap4 was kinetically and thermodynamically more...

The influence of the chlorine-hydrogen ratio in the gas phase on the stability of the {113} faces of silicon in Si-H-Cl CVD

1990 ◽  
Vol 102 (1-2) ◽  
pp. 233-244 ◽  
Author(s):  
J.G.E. Gardeniers ◽  
M.M.W. Mooren ◽  
M.H.J.M. De Croon ◽  
L.J. Giling
Keyword(s):  
Gas Phase ◽  
The Stability

scholarly journals Catalytic Performance of Nitrogen-Doped Activated Carbon Supported Pd Catalyst for Hydrodechlorination of 2,4-Dichlorophenol or Chloropentafluoroethane

Molecules ◽  
2019 ◽  
Vol 24 (4) ◽  
pp. 674 ◽  
Author(s):  
Haodong Tang ◽  
Bin Xu ◽  
Meng Xiang ◽  
Xinxin Chen ◽  
Yao Wang ◽  
...  
Keyword(s):  
Activated Carbon ◽  
Liquid Phase ◽  
Gas Phase ◽  
Nitrogen Doping ◽  
Catalyst Surface ◽  
Catalytic Performance ◽  
Atomic Ratio ◽  
Pd Catalyst ◽  
Nitrogen Doped ◽  
The Stability

Nitrogen-doped activated carbon (N-AC) obtained through the thermal treatment of a mixture of HNO3-pretreated activated carbon (AC) and urea under N2 atmosphere at 600 °C was used as the carrier of Pd catalyst for both liquid-phase hydrodechlorination of 2,4-dichlorophenol (2,4-DCP) and gas-phase hydrodechlorination of chloropentafluoroethane (R-115). The effects of nitrogen doping on the dispersion and stability of Pd, atomic ratio of Pd/Pd2+ on the surface of the catalyzer, the catalyst’s hydrodechlorination activity, as well as the stability of N species in two different reaction systems were investigated. Our results suggest that, despite no improvement in the dispersion of Pd, nitrogen doping may significantly raise the atomic ratio of Pd/Pd2+ on the catalyst surface, with a value of 1.2 on Pd/AC but 2.2 on Pd/N-AC. Three types of N species, namely graphitic, pyridinic, and pyrrolic nitrogen, were observed on the surface of Pd/N-AC, and graphitic nitrogen was stable in both liquid-phase hydrodechlorination of 2,4-DCP and gas-phase hydrodechlorination of R-115, with pyridinic and pyrrolic nitrogen being unstable during gas-phase hydrodechlorination of R-115. As a result, the average size of Pd nanocrystals on Pd/N-AC was almost kept unchanged after liquid-phase hydrodechlorination of 2,4-DCP, whereas crystal growth of Pd was clearly observed on Pd/N-AC after gas-phase hydrodechlorination of R-115. The activity test revealed that Pd/N-AC exhibited a much better performance than Pd/AC in liquid-phase hydrodechlorination of 2,4-DCP, probably due to the enhanced stability of Pd exposed to the environment resulting from nitrogen doping as suggested by the higher atomic ratio of Pd/Pd2+ on the catalyst surface. In the gas-phase hydrodechlorination of R-115, however, a more rapid deactivation phenomenon occurred on Pd/N-AC than on Pd/AC despite a higher activity initially observed on Pd/N-AC, hinting that the stability of pyridinic and pyrrolic nitrogen plays an important role in the determination of catalytic performance of Pd/N-AC.

scholarly journals Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Traveling Wave Device

2019 ◽  
Vol 91 (12) ◽  
pp. 7554-7561 ◽  
Author(s):  
Charles Eldrid ◽  
Jakub Ujma ◽  
Symeon Kalfas ◽  
Nick Tomczyk ◽  
Kevin Giles ◽  
...  
Keyword(s):  
Gas Phase ◽  
Ion Mobility Spectrometry ◽  
Phase Stability ◽  
Ion Mobility ◽  
Traveling Wave ◽  
Protein Ions ◽  
Wave Device

Do electrospray mass spectra reflect the ligand binding state of proteins in solution?

2005 ◽  
Vol 83 (11) ◽  
pp. 1953-1960 ◽  
Author(s):  
Belal M Hossain ◽  
Douglas A Simmons ◽  
Lars Konermann
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Protein Interactions ◽  
Noncovalent Complex ◽  
Deuterium Exchange ◽  
Solution Phase ◽  
Hydrogen Deuterium Exchange ◽  
Esi Ms ◽  
Protein Ions ◽  
Hydrogen Deuterium

Electrospray ionization (ESI) mass spectrometry (MS) has become a popular tool for monitoring ligand–protein and protein–protein interactions. Due to the "gentle" nature of the ionization process, it is often possible to transfer weakly bound complexes into the gas phase, thus making them amenable to MS detection. One problem with this technique is the potential occurrence of fragmentation events during ESI. Also, some analytes tend to cluster together during ionization, thus forming nonspecific gas-phase assemblies that do not represent solution-phase complexes. In this work, we implemented a hydrogen–deuterium exchange (HDX) approach that can reveal whether or not the free and (or) bound constituents of a complex observed in ESI-MS reflect the binding situation in solution. Proteins are subjected to ESI immediately following an isotopic labeling pulse; only ligand-free and ligand-bound protein ions that were formed directly from the corresponding solution-phase species showed different HDX levels. Using myoglobin as a model system, it is demonstrated that this approach can readily distinguish scenarios where the heme–protein interactions were disrupted in solution from those where dissociation of the complex occurred in the gas phase. Experiments on cytochrome c strongly suggest that dimeric protein ions observed in ESI-MS reflect aggregates that were formed in solution.Key words: electrospray mass spectrometry, ligand–protein interaction, noncovalent complex, hydrogen–deuterium exchange, protein folding.

Sign in / Sign up

Export Citation Format

Share Document