Wood T D, Chorush R A, Wampler F M, Little D P, O'Connor P B, McLafferty F W
Baker Chemistry Laboratory, Cornell University, Ithaca, NY 14853-1301, USA.
Proc Natl Acad Sci U S A. 1995 Mar 28;92(7):2451-4. doi: 10.1073/pnas.92.7.2451.
Water is thought to play a dominant role in protein folding, yet gaseous multiply protonated proteins from which the water has been completely removed show hydrogen/deuterium (H/D) exchange behavior similar to that used to identify conformations in solution. Indicative of the gas-phase accessibility to D2O, multiply-charged (6+ to 17+) cytochrome c cations exchange at six (or more) distinct levels of 64 to 173 out of 198 exchangeable H atoms, with the 132 H level found at charge values 8+ to 17+. Infrared laser heating and fast collisions can apparently induce ions to unfold to exchange at a higher distinct level, while charge-stripping ions to lower charge values yields apparent folding as well as unfolding.
水被认为在蛋白质折叠过程中起主要作用,然而,完全去除了水的气态多质子化蛋白质表现出的氢/氘(H/D)交换行为,与用于识别溶液中构象的行为相似。多电荷(6+至17+)细胞色素c阳离子对D2O的气相可及性表明,在198个可交换氢原子中,有64至173个以六个(或更多)不同水平进行交换,在电荷值为8+至17+时发现132H水平。红外激光加热和快速碰撞显然可以诱导离子展开,以在更高的不同水平进行交换,而将离子电荷剥离至较低电荷值会产生明显的折叠以及展开。