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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >K-edge anomalous SAXS for protein solution structure modeling
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K-edge anomalous SAXS for protein solution structure modeling

机译:K-edge异常粉煤灰对蛋白质的解决方案结构建模

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摘要

K-edge anomalous SAXS intensity was measured from a small, dimeric, partly unstructured protein segment of myosin X by using cupric ions bound to its C-terminal polyhistidine tags. Energy-dependent anomalous SAXS can provide key location-specific information about metal-labeled protein structures in solution that cannot be obtained from routine SAXS analysis. However, anomalous SAXS is seldom used for protein research due to practical difficulties, such as a lack of generic multivalent metal-binding tags and the challenges of measuring weak anomalous signal at the metal absorption edge. This pilot feasibility study suggests that weak K-edge anomalous SAXS signal can be obtained from transition metals bound to terminally located histidine tags of small proteins. The measured anomalous signal can provide information about the distribution of all metal-protein distances in the complex. Such an anomalous SAXS signal can assist in the modeling and validation of structured or unstructured proteins in solution and may potentially become a new addition to the repertoire of techniques in integrative structural biology.
机译:K-edge异常粉煤灰强度测量小二聚的,部分非结构化的蛋白质段肌凝蛋白绑定到X用铜离子它的c端polyhistidine标签。依赖资源异常一枝可以提供关键具体地点的信息metal-labeled不能在溶液中蛋白质结构从常规获得一枝分析。异常一枝很少用于蛋白质研究由于实际困难,比如缺乏通用的多价metal-binding标签和测量弱异常的挑战信号在金属吸收边。可行性研究表明K-edge疲软可以获得一枝异常信号过渡金属绑定到晚期组氨酸标签的蛋白质。异常信号可以提供的信息所有metal-protein距离的分布在复杂。协助的建模和验证结构化或非结构化蛋白质在溶液中并可能成为新成员在综合的技术结构生物学。

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