title: How ubiquitin unfolds after transfer into the gas phase.
abstract: 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.
authors.affiliation: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
authors.forename: Owen S
authors.initials: OS
authors.lastname: Skinner
authors.forename: Fred W
authors.initials: FW
authors.lastname: McLafferty
authors.forename: Kathrin
authors.initials: K
authors.lastname: Breuker
mesh_terms: D005740:Gases / Q000737:chemistry; D006860:Hydrogen Bonding; D013058:Mass Spectrometry; D011487:Protein Conformation; D055550:Protein Stability; D058767:Protein Unfolding; D055672:Static Electricity; D025801:Ubiquitin / Q000737:chemistry* / Q000378:metabolism
chemical_list: D005740:Gases; D025801:Ubiquitin