Hydration water dynamics in bovine serum albumin at low temperatures as studied by deuterium solid-state NMR
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文摘

Changes in the structure and dynamics of hydration waters due to glass transitions were investigated for bovine serum albumin by solid state 2H NMR.

The isotropic rotation of water molecules near the protein was restricted by freezing of the disordered region in the protein around Tg=200 K.

A 180° flip becomes the dominant motion for water molecules near protein below Tg = 200 K.

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