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
SN - 1387-3806
VL - 338
SP - 2
EP - 10
JO - International Journal of Mass Spectrometry
JF - International Journal of Mass Spectrometry
ER -