Temperature dependence of gas-phase conformations for ubiquitin ions characterized by proton transfer reactions

Nonose, Shinji; Okamura, Takuya; Yamashita, Kazuki; Sudo, Ayako

doi:10.1016/j.chemphys.2013.02.009

Cited by 7 publications

(14 citation statements)

References 45 publications

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“…Details of the experimental apparatus used in the present study have been described elsewhere. [15][16][17] Brie y, the system consists of four vacuum chambers with an ESI source, a tandem mass spectrometer, and a gas cell equipped with an octapole ion trap. Multiply-protonated peptide and protein ions were produced by ESI.…”

Section: Methodsmentioning

confidence: 99%

“…Details of scheme used to determine absolute values of the rate constants have been described elsewhere. 16,17) In Fig. 2, the reaction rate constants for proton transfer from [Ang+2H] 2+ , to 1-Bu, dipropylamine (Dpr), 3,5-dimethylpyridine 30) (35Dmpy), and 2,6-dimethylpyridine (26Dmpy) are plotted as a function of temperature in the gas cell.…”

Section: Angiotension Imentioning

confidence: 99%

“…Proton transfer from multiply-protonated ubiquitin ions, [Ubi+zH] z+ (z=6-12), to 1-Bu was examined in the gas phase. 17) Absolute reaction rate constant for proton transfer was determined from the intensities of parent and product ions in the mass spectra. In Fig.…”

Section: Ubiquitinmentioning

confidence: 99%

“…e structures and reactions of gas-phase biomolecules have been studied extensively using various mass spectrometric methods. [8][9][10][11][12][13][14][15][16][17] Protein conformations and dynamics have been studied extensively by mass spectrometry-based approaches to characterize kinetic intermediates in refolding experiments. A new experimental approach would be expected to allow exact biomolecular structures to be determined in the gas phase.…”

Section: Introductionmentioning

confidence: 99%

“…10) Proton transfer reactions of angiotensin I, disul de-intact and -reduced lysozyme, and ubiquitin ions for multiplyprotonated states are discussed in this study. [15][16][17] e temperature dependence of the absolute reaction rate constant for proton transfer and the distribution of product ions were examined for those peptide and protein ions in the gas phase. An issue that is attracting considerable attention is their gas-phase conformations that could resemble structural evolution that originated from temperature in the gas phase.…”

Section: Introductionmentioning

confidence: 99%

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Temperature-Resolved Proton Transfer Reactions of Biomolecular Ions

Nonose

2020

Mass Spectrometry

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Temperature-resolved proton transfer reactions of multiply-protonated angiotensin I, disul de-intact and-reduced lysozyme, and ubiquitin ions to primary, secondary and aromatic amines were examined in the gas phase. Absolute reaction rate constants for the proton transfer were determined from the intensities of the parent and product ions in mass spectra. Dramatic changes were observed in the distribution of product ions and the reaction rate constants. In particular, the rate constants for disul de-intact lysozyme ions changed more drastically with the change in charge state and temperature compared to the corresponding values for disul de-reduced ions. Proton transfer reactions were enhanced or suppressed as the result of the formation of complexes between the ions with gaseous molecules, which is related to changes in their conformation with changing.

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Section: Methodsmentioning

confidence: 99%

Section: Angiotension Imentioning

confidence: 99%

Section: Ubiquitinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Temperature-Resolved Proton Transfer Reactions of Biomolecular Ions

Nonose

2020

Mass Spectrometry

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Proton transfer and complex formation of angiotensin I ions with gaseous molecules at various temperature

et al. 2013

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Gas-Phase Acidities of Phosphorylated Amino Acids

et al. 2015

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Gas-phase acidities and heats of formation have been predicted at the G3(MP2)/SCRF-COSMO level of theory for 10 phosphorylated amino acids and their corresponding amides, including phospho-serine (pSer), -threonine (pThr), and -tyrosine (pTyr), providing the first reliable set of these values. The gas-phase acidities (GAs) of the three named phosphorylated amino acids and their amides have been determined using proton transfer reactions in a Fourier transform ion cyclotron mass spectrometer. Excellent agreement was found between the experimental and predicted GAs. The phosphate group is the deprotonation site for pSer and pThr and deprotonation from the carboxylic acid generated the lowest energy anion for pTyr. The infrared spectra were calculated for six low energy anions of pSer, pThr, and pTyr. For deprotonated pSer and pThr, good agreement is found between the experimental IRMPD spectra and the calculated spectra for our lowest energy anion structure. For pTyr, the IR spectra for a higher energy phosphate deprotonated structure is in good agreement with experiment. Additional experiments tested electrospray ionization (ESI) conditions for pTyr and determined that variations in solvent, temperature, and voltage can result in a different experimental GA value, indicating that ESI conditions affect the conformation of the pTyr anion.

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Temperature dependence of gas-phase conformations for ubiquitin ions characterized by proton transfer reactions

Cited by 7 publications

References 45 publications

Temperature-Resolved Proton Transfer Reactions of Biomolecular Ions

Temperature-Resolved Proton Transfer Reactions of Biomolecular Ions

Proton transfer and complex formation of angiotensin I ions with gaseous molecules at various temperature

Gas-Phase Acidities of Phosphorylated Amino Acids

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