Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry. / Bache, Nicolai; Rand, Kasper Dyrberg; Roepstorff, Peter; Ploug, Michael; Jørgensen, Thomas.

In: Journal of The American Society for Mass Spectrometry, Vol. 19, No. 12, 2008, p. 1719-25.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Bache, N, Rand, KD, Roepstorff, P, Ploug, M & Jørgensen, T 2008, 'Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry', Journal of The American Society for Mass Spectrometry, vol. 19, no. 12, pp. 1719-25. https://doi.org/10.1016/j.jasms.2008.05.021

APA

Bache, N., Rand, K. D., Roepstorff, P., Ploug, M., & Jørgensen, T. (2008). Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry. Journal of The American Society for Mass Spectrometry, 19(12), 1719-25. https://doi.org/10.1016/j.jasms.2008.05.021

Vancouver

Bache N, Rand KD, Roepstorff P, Ploug M, Jørgensen T. Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry. Journal of The American Society for Mass Spectrometry. 2008;19(12):1719-25. https://doi.org/10.1016/j.jasms.2008.05.021

Author

Bache, Nicolai ; Rand, Kasper Dyrberg ; Roepstorff, Peter ; Ploug, Michael ; Jørgensen, Thomas. / Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry. In: Journal of The American Society for Mass Spectrometry. 2008 ; Vol. 19, No. 12. pp. 1719-25.

Bibtex

@article{132835f2615b4588ab49b331a0c736bc,
title = "Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry",
abstract = "We have previously shown that peptide amide hydrogens undergo extensive intramolecular migration (i.e., complete hydrogen scrambling) upon collisional activation of protonated peptides (J{\o}rgensen et al. J. Am. Chem. Soc. 2005, 127, 2785-2793). The occurrence of hydrogen scrambling enforces severe limitations on the application of gas-phase fragmentation as a convenient method to obtain information about the site-specific deuterium uptake for proteins and peptides in solution. To investigate whether deprotonated peptides exhibit a lower level of scrambling relative to their protonated counterparts, we have now measured the level of hydrogen scrambling in a deprotonated, selectively labeled peptide using MALDI tandem time-of-flight mass spectrometry. Our results conclusively show that hydrogen scrambling is prevalent in the deprotonated peptide upon collisional activation. The amide hydrogens ((1)H/(2)H) have migrated extensively in the anionic peptide, thereby erasing the original regioselective deuteration pattern obtained in solution.",
keywords = "Amino Acid Sequence, Anions, Crystallography, X-Ray, Humans, Hydrogen, Models, Molecular, Oligopeptides, Peptides, Protein Structure, Tertiary, Receptors, Urokinase Plasminogen Activator, Recombinant Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Tandem Mass Spectrometry",
author = "Nicolai Bache and Rand, {Kasper Dyrberg} and Peter Roepstorff and Michael Ploug and Thomas J{\o}rgensen",
year = "2008",
doi = "10.1016/j.jasms.2008.05.021",
language = "English",
volume = "19",
pages = "1719--25",
journal = "Journal of The American Society for Mass Spectrometry",
issn = "1044-0305",
publisher = "Springer Nature",
number = "12",

}

RIS

TY - JOUR

T1 - Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry

AU - Bache, Nicolai

AU - Rand, Kasper Dyrberg

AU - Roepstorff, Peter

AU - Ploug, Michael

AU - Jørgensen, Thomas

PY - 2008

Y1 - 2008

N2 - We have previously shown that peptide amide hydrogens undergo extensive intramolecular migration (i.e., complete hydrogen scrambling) upon collisional activation of protonated peptides (Jørgensen et al. J. Am. Chem. Soc. 2005, 127, 2785-2793). The occurrence of hydrogen scrambling enforces severe limitations on the application of gas-phase fragmentation as a convenient method to obtain information about the site-specific deuterium uptake for proteins and peptides in solution. To investigate whether deprotonated peptides exhibit a lower level of scrambling relative to their protonated counterparts, we have now measured the level of hydrogen scrambling in a deprotonated, selectively labeled peptide using MALDI tandem time-of-flight mass spectrometry. Our results conclusively show that hydrogen scrambling is prevalent in the deprotonated peptide upon collisional activation. The amide hydrogens ((1)H/(2)H) have migrated extensively in the anionic peptide, thereby erasing the original regioselective deuteration pattern obtained in solution.

AB - We have previously shown that peptide amide hydrogens undergo extensive intramolecular migration (i.e., complete hydrogen scrambling) upon collisional activation of protonated peptides (Jørgensen et al. J. Am. Chem. Soc. 2005, 127, 2785-2793). The occurrence of hydrogen scrambling enforces severe limitations on the application of gas-phase fragmentation as a convenient method to obtain information about the site-specific deuterium uptake for proteins and peptides in solution. To investigate whether deprotonated peptides exhibit a lower level of scrambling relative to their protonated counterparts, we have now measured the level of hydrogen scrambling in a deprotonated, selectively labeled peptide using MALDI tandem time-of-flight mass spectrometry. Our results conclusively show that hydrogen scrambling is prevalent in the deprotonated peptide upon collisional activation. The amide hydrogens ((1)H/(2)H) have migrated extensively in the anionic peptide, thereby erasing the original regioselective deuteration pattern obtained in solution.

KW - Amino Acid Sequence

KW - Anions

KW - Crystallography, X-Ray

KW - Humans

KW - Hydrogen

KW - Models, Molecular

KW - Oligopeptides

KW - Peptides

KW - Protein Structure, Tertiary

KW - Receptors, Urokinase Plasminogen Activator

KW - Recombinant Proteins

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

KW - Tandem Mass Spectrometry

U2 - 10.1016/j.jasms.2008.05.021

DO - 10.1016/j.jasms.2008.05.021

M3 - Journal article

C2 - 18640053

VL - 19

SP - 1719

EP - 1725

JO - Journal of The American Society for Mass Spectrometry

JF - Journal of The American Society for Mass Spectrometry

SN - 1044-0305

IS - 12

ER -

ID: 40129835