Multi-step evolution of protein conformation on electrospray into the gas phase.
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.
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA. fwm5@cornell.edu
Fred W
FW
McLafferty
Sergio
S
Castro
Kathrin
K
Breuker
D003903:Deuterium; D005740:Gases / Q000032:analysis; D006859:Hydrogen; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D025801:Ubiquitin / Q000737:chemistry*; D014867:Water
D005740:Gases; D011506:Proteins; D025801:Ubiquitin; D014867:Water; D006859:Hydrogen; D003903:Deuterium