共 32 条
Multi-step evolution of protein conformation on electrospray into the gas phase
被引:11
作者:
McLafferty, Fred W.
[1
]
Castro, Sergio
[1
]
Breuker, Kathrin
[2
,3
]
机构:
[1] Cornell Univ, Dept Chem & Chem Biol, Ithaca, NY 14853 USA
[2] Univ Innsbruck, Inst Organ Chem, A-6020 Innsbruck, Austria
[3] Univ Innsbruck, Ctr Mol Biosci Innsbruck, A-6020 Innsbruck, Austria
关键词:
gaseous protein conformation;
H/D exchange;
etectrospray;
protein folding;
NATIVE CYTOCHROME-C;
CAPTURE DISSOCIATION;
MASS-SPECTROMETRY;
STRUCTURAL-CHARACTERIZATION;
TOP-DOWN;
IONS;
IONIZATION;
TRANSITION;
COMPLEXES;
MOLECULE;
D O I:
10.1255/ejms.1058
中图分类号:
O64 [物理化学(理论化学)、化学物理学];
O56 [分子物理学、原子物理学];
学科分类号:
070203 ;
070304 ;
081704 ;
1406 ;
摘要:
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/deuterium exchange is the opposite, with ubiquitin 7+ and 13+ ions exchanging >60D and -15D 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.
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页码:437 / 442
页数:6
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