McLafferty Fred W, Castro Sergio, Breuker Kathrin
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
Eur J Mass Spectrom (Chichester). 2010;16(3):437-42. doi: 10.1255/ejms.1058.
In the gas phase, some properties of native versus denatured protein conformations correspond to those in solution, such as affinity for protons and physical cross section. However, the capacity for hydrogen/deutrerium exchange is the opposite, with ubiquitin 7+ and 13+ ions exchanging >-60 D and approximately 15 D atoms, respectively. A variety of experimental methods now delineate a series of conformational perturbations that can occur in the 10(-12) s to 10(+2) s following electrospray, including side-chain collapse, hydrophobic and electrostatic non-covalent bond unfolding and refolding into a variety of non-native structures.
