Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry

Research output: Contribution to journal › Review › Research › peer-review

Standard

Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry. / Rand, Kasper Dyrberg.

In: International Journal of Mass Spectrometry, Vol. 338, 15.03.2013, p. 2-10.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Rand, KD 2013, 'Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry', International Journal of Mass Spectrometry, vol. 338, pp. 2-10. https://doi.org/10.1016/j.ijms.2012.08.010

APA

Rand, K. D. (2013). Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry. International Journal of Mass Spectrometry, 338, 2-10. https://doi.org/10.1016/j.ijms.2012.08.010

Vancouver

Rand KD. Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry. International Journal of Mass Spectrometry. 2013 Mar 15;338:2-10. https://doi.org/10.1016/j.ijms.2012.08.010

Author

Rand, Kasper Dyrberg. / Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry. In: International Journal of Mass Spectrometry. 2013 ; Vol. 338. pp. 2-10.

Bibtex

@article{f1bb86a99f8a4383ad6b4eff9cb78096,
title = "Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry",
abstract = "This Feature describes the use of electron transfer dissociation (ETD) to analyze the hydrogen/deuterium exchange (HDX) of proteins at increased spatial resolution down to the level of individual residues. A practical overview of how to couple ETD to the classical bottom-up HDX-MS workflow is given and new options for method optimization are discussed and exemplified. In addition, the real-world applicability of the HDX-ETD method to pinpoint conformational changes in a large 75 kDa protein complex of therapeutic interest is demonstrated. This feature highlights how the conformation and interactions of complex protein systems of biological or pharmaceutical interest can now be analyzed at a hitherto unprecedented level of structural detail using an MS-based method.",
author = "Rand, {Kasper Dyrberg}",
year = "2013",
month = mar,
day = "15",
doi = "10.1016/j.ijms.2012.08.010",
language = "English",
volume = "338",
pages = "2--10",
journal = "International Journal of Mass Spectrometry",
issn = "1387-3806",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry

AU - Rand, Kasper Dyrberg

PY - 2013/3/15

Y1 - 2013/3/15

N2 - This Feature describes the use of electron transfer dissociation (ETD) to analyze the hydrogen/deuterium exchange (HDX) of proteins at increased spatial resolution down to the level of individual residues. A practical overview of how to couple ETD to the classical bottom-up HDX-MS workflow is given and new options for method optimization are discussed and exemplified. In addition, the real-world applicability of the HDX-ETD method to pinpoint conformational changes in a large 75 kDa protein complex of therapeutic interest is demonstrated. This feature highlights how the conformation and interactions of complex protein systems of biological or pharmaceutical interest can now be analyzed at a hitherto unprecedented level of structural detail using an MS-based method.

AB - This Feature describes the use of electron transfer dissociation (ETD) to analyze the hydrogen/deuterium exchange (HDX) of proteins at increased spatial resolution down to the level of individual residues. A practical overview of how to couple ETD to the classical bottom-up HDX-MS workflow is given and new options for method optimization are discussed and exemplified. In addition, the real-world applicability of the HDX-ETD method to pinpoint conformational changes in a large 75 kDa protein complex of therapeutic interest is demonstrated. This feature highlights how the conformation and interactions of complex protein systems of biological or pharmaceutical interest can now be analyzed at a hitherto unprecedented level of structural detail using an MS-based method.

U2 - 10.1016/j.ijms.2012.08.010

DO - 10.1016/j.ijms.2012.08.010

M3 - Review

VL - 338

SP - 2

EP - 10

JO - International Journal of Mass Spectrometry

JF - International Journal of Mass Spectrometry

SN - 1387-3806

ER -

ID: 49607832