Electron capture dissociation;
Protein;
Ubiquitin;
Gas phase structure;
ELECTRON-CAPTURE DISSOCIATION;
NATIVE CYTOCHROME-C;
MASS-SPECTROMETRY;
NONCOVALENT INTERACTIONS;
PROTEIN CATIONS;
LIGAND-BINDING;
TOP-DOWN;
IONS;
TRANSITIONS;
ENVIRONMENT;
D O I:
10.1007/s13361-012-0370-6
中图分类号:
Q5 [生物化学];
学科分类号:
071010 ;
081704 ;
摘要:
The structural evolution of ubiquitin after transfer into the gas phase was studied by electron capture dissociation. Site-specific fragment yields show that ubiquitin's solution fold is overall unstable in the gas phase, but unfolding caused by loss of solvent is slowest in regions stabilized by salt bridges.