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- W2036704611 abstract "Using a combination of $^{2}mathrm{H}$ nuclear magnetic resonance (NMR) methods, we study internal rotational dynamics of the perdeuterated protein C-phycocyanin (CPC) in dry and hydrated states over broad temperature and dynamic ranges with high angular resolution. Separating $^{2}mathrm{H}$ NMR signals from methyl deuterons, we show that basically all backbone deuterons exhibit highly restricted motion occurring on time scales faster than microseconds. The amplitude of this motion increases when a hydration shell exists, while it decreases upon cooling and vanishes near 175 K. We conclude that the vanishing of the highly restricted motion marks a dynamical transition, which is independent of the time window and of a fundamental importance. This conclusion is supported by results from experimental and computational studies of the proteins myoglobin and elastin. In particular, we argue based on findings in molecular dynamics simulations that the behavior of the highly restricted motion of proteins at the dynamical transition resembles that of a characteristic secondary relaxation of liquids at the glass transition, namely the nearly constant loss. Furthermore, $^{2}mathrm{H}$ NMR studies on perdeuterated CPC reveal that, in addition to highly restricted motion, small fractions of backbone segments exhibit weakly restricted dynamics when temperature and hydration are sufficiently high." @default.
- W2036704611 created "2016-06-24" @default.
- W2036704611 creator A5001598276 @default.
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- W2036704611 date "2014-03-17" @default.
- W2036704611 modified "2023-10-01" @default.
- W2036704611 title "Vanishing amplitude of backbone dynamics causes a true protein dynamical transition:<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mmultiscripts><mml:mi mathvariant=normal>H</mml:mi><mml:mprescripts /><mml:none /><mml:mrow><mml:mn>2</mml:mn></mml:mrow></mml:mmultiscripts></mml:math>NMR studies on perdeuterated C-phycocyanin" @default.
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- W2036704611 doi "https://doi.org/10.1103/physreve.89.032710" @default.
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