Solution structure of a minor and transiently formed state of a T4 lysozyme mutant

摘要

Proteins are inherently plastic molecules, whose function often critically depends on excursions between different molecular conformations (conformers)1"3. However, a rigorous understanding of the relation between a protein's structure, dynamics and function remains elusive. This is because many of the conformers on its energy landscape are only transiently formed and marginally populated (less than a few per cent of the total number of molecules), so that they cannot be individually characterized by most biophysical tools.%一个蛋白的功能，极大地取决于其结构动态以及蛋白分子可以采取的过渡构形中间体的性质。这些过渡结构会是难以把握的，因此也难以定性。这篇论文报告，研究人员将弛豫-色散核磁共振与Rosetta计算结构预测结合起来，设计T4溶菌酶突变，后者能够稳定那些通常瞬时性太强而难以观测的“激发”态。