无定形固体
化学物理
分子
玻璃化转变
原籍国
化学
灵活性(工程)
蛋白质动力学
化学稳定性
分子动力学
功能(生物学)
热力学
结晶学
材料科学
聚合物
物理
计算化学
有机化学
统计
数学
进化生物学
生物
作者
John J. Hill,Evgenyi Shalaev,George Zografi
摘要
Abstract
The internal, dynamical fluctuations of protein molecules exhibit many of the features typical of polymeric and bulk small molecule glass forming systems. The response of a protein's internal molecular mobility to temperature changes is similar to that of other amorphous systems, in that different types of motions freeze out at different temperatures, suggesting they exhibit the α-β-modes of motion typical of polymeric glass formers. These modes of motion are attributed to the dynamic regimes that afford proteins the flexibility for function but that also develop into the large-scale collective motions that lead to unfolding. The protein dynamical transition, Td, which has the same meaning as the Tg value of other amorphous systems, is attributed to the temperature where protein activity is lost and the unfolding process is inhibited. This review describes how modulation of Td by hydration and lyoprotectants can determine the stability of protein molecules that have been processed as bulk, amorphous materials. It also examines the thermodynamic, dynamic, and molecular factors involved in stabilizing folded proteins, and the effects typical pharmaceutical processes can have on native protein structure in going from the solution state to the solid state.
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