Solid-state NMR studies of the structure and mechanisms of proteins.
Solid-state NMR studies of the structure and mechanisms of proteins.
复制标题
蛋白质结构和机制的固态核磁共振研究。
DOI：
10.1016/s0959-440x(02)00374-3
复制
发表时间：
2002
影响因子：
6.8
通讯作者：
Thompson,LynmarieK
中科院分区：
文献类型：
--
作者：
Thompson,LynmarieK
魔角旋转固态核磁共振实验非常适合研究 X 射线晶体学和溶液核磁共振波谱无法获得的重要蛋白质的结构和机制，包括膜蛋白和与疾病相关的蛋白质聚集体。在开发使用统一 13 C、 15 N 标记样品来完整测定小（<20 kDa）固体蛋白结构的方法方面已取得良好进展。针对标记活性位点的选择性标记蛋白质的研究已经深入了解参与能量和信号转导的酶和膜蛋白的机制。对选择性标记合成肽的研究已经产生了生物医学重要系统的结构模型，包括淀粉样原纤维和参与生物矿化和细胞粘附的表面相关肽。新型核磁共振和生化方法正在开发中，以针对大型蛋白质和全细胞内的固态核磁共振实验。这些方法被用来研究膜受体跨膜信号传导的机制，并表征抗生素和细菌细胞壁之间的结合相互作用。因此，固态核磁共振被证明是一种有价值的生物物理工具，可用于探测各种生物分子的结构和动力学。
Magic-angle spinning solid-state NMR experiments are well suited to investigating the structures and mechanisms of important proteins that are inaccessible to X-ray crystallography and solution NMR spectroscopy, including membrane proteins and disease-related protein aggregates. Good progress has been made in the development of methods for the complete structure determination of small (<20 kDa) solid proteins using uniformly13C,15N-labeled samples. Studies of selectively labeled proteins focusing on labeled active sites have yielded insights into the mechanisms of enzymes and of membrane proteins involved in energy and signal transduction. Studies of selectively labeled synthetic peptides have yielded structural models for biomedically important systems, including amyloid fibrils and surface-associated peptides involved in biomineralization and cell adhesion. Novel NMR and biochemical methods are being developed to target solid-state NMR experiments within large proteins and whole cells. These approaches are being used to investigate mechanisms of transmembrane signaling by membrane receptors and to characterize binding interactions between antibiotics and bacterial cell walls. Thus, solid-state NMR is proving to be a valuable biophysical tool for probing structure and dynamics in a wide range of biomolecules.