破坏酶的流动性。
Disrupting enzyme fluidity.
机构信息
Department of Chemistry and Huck Institute of Life Sciences, Pennsylvania State University, University Park, United States.
出版信息
Elife. 2021 Jan 25;10:e65221. doi: 10.7554/eLife.65221.
Abstract
A combination of X-ray crystallography, NMR, and mass spectrometry has revealed how diverse small-molecule inhibitors bind Bruton's tyrosine kinase and alter the conformation of this enzyme.
摘要
X 射线晶体学、NMR 和质谱的组合揭示了不同的小分子抑制剂如何结合布鲁顿酪氨酸激酶并改变该酶的构象。
Zotero 插件