Inelastic X-ray Scattering Studies of the Short-Time Collective Vibrational Motions in Hydrated Lysozyme Powders and Their Possible Relation to Enzymatic Function
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文摘
High-resolution inelastic X-ray scattering was used to investigate the collective vibrational excitations in hydrated lysozyme powders as a function of hydration level and temperature. It is found that the samples with strong enzymatic function are 鈥渟oft鈥? in the sense that they exhibit low frequency and large amplitude intraprotein collective vibrational motions on certain length scales. This is not the case for samples with weak or no enzymatic activity. Thus, we identify a possible correlation between the short-time intraprotein collective vibrational motions and the establishment of enzymatic function in hydrated lysozyme powders, and bring new insight to notions of protein 鈥渃onformational flexibility鈥?and 鈥渟oftness鈥?in terms of these motions.

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