Das Rahul K, Ruff Kiersten M, Pappu Rohit V
Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, One Brookings Drive, Campus Box 1097, St. Louis, MO 63130, USA.
Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, One Brookings Drive, Campus Box 1097, St. Louis, MO 63130, USA.
Curr Opin Struct Biol. 2015 Jun;32:102-12. doi: 10.1016/j.sbi.2015.03.008. Epub 2015 Apr 2.
Intrinsically disordered proteins (IDPs) showcase the importance of conformational plasticity and heterogeneity in protein function. We summarize recent advances that connect information encoded in IDP sequences to their conformational properties and functions. We focus on insights obtained through a combination of atomistic simulations and biophysical measurements that are synthesized into a coherent framework using polymer physics theories.
内在无序蛋白（IDP）展现了构象可塑性和异质性在蛋白质功能中的重要性。我们总结了近期的进展，这些进展将IDP序列中编码的信息与其构象性质和功能联系起来。我们着重介绍通过原子模拟和生物物理测量相结合所获得的见解，这些见解利用聚合物物理理论被整合到一个连贯的框架中。
