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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >An investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C.
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An investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C.

机译:调查的质子化作用状态心脏的C1领域myosin-binding蛋白质C。

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摘要

Myosin-binding protein C (MyBP-C) is a myofibril-associated protein found in cardiac and skeletal muscle. The cardiac isoform (cMyBP-C) is subject to reversible phosphorylation and the surface-charge state of the protein is of keen interest with regard to understanding the inter-protein interactions that are implicated in its function. Diffraction data from the C1 domain of cMyBP-C were extended to 1.30 A resolution, where the of the diffraction data crosses 2.0, using intense synchrotron radiation. The protonation-state determinations were not above 2sigma (the best was 1.81sigma) and therefore an extrapolation is given, based on 100% data completeness and the average DPI, that a 3sigma determination could be possible if X-ray data could be measured to 1.02 A resolution. This might be possible via improved crystallization or multiple sample evaluation, e.g. using robotics or a yet more intense/collimated X-ray beam or combinations thereof. An alternative would be neutron protein crystallography at 2 A resolution, where it is estimated that for the unit-cell volume of the cMyBP-C C1 domain crystal a crystal volume of 0.10 mm3 would be needed with fully deuterated protein on LADI III. These efforts would optimally be combined in a joint X-ray and neutron model refinement.
机译:Myosin-binding蛋白C (MyBP-C)myofibril-associated蛋白质存在于心脏和骨骼肌。可逆的磷酸化和主题表面电荷的蛋白质是敏锐的关于理解的兴趣inter-protein涉及的交互它的功能。cMyBP-C被扩展到1.30一项决议,在的衍射数据穿过2.0,使用强烈的同步辐射。protonation-state决定没有以上2σ(最好的是1.81σ)和因此一个推断,基于数据完整性和平均DPI, 100%3σ的决心可能如果x射线1.02数据可以测量分辨率。可能通过改善结晶或多个样品评估,如使用机器人或更多强烈的/平行x射线或组合。中子蛋白质晶体学2决议,是估计的晶胞体积cMyBP-C C1域的晶体晶体体积0.10 mm3的需要完全氘蛋白质LADI三世。努力将在联合优化组合x射线和中子模型细化。

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