【摘 要】
：
Flexibility between domains within a multi-domain protein is often critical for its biological function.This paper presents a comprehensive investigation to
【机 构】
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合肥微尺度物质科学国家实验室和中国科学技术大学生命科学学院,合肥230026
【出 处】
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2013年第四届全国“跨学科蛋白质研究”学术讨论会
论文部分内容阅读
Flexibility between domains within a multi-domain protein is often critical for its biological function.This paper presents a comprehensive investigation to the structural flexibility between the two tandem WW domains in formin binding protein 21 (FBP21-WWs), via an integrative method of using both computational simulations and experimental data from small angle X-ray scattering (SAXS).
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