Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins. (October 2019)

• Record Type: Journal Article
• Authors: Arthanari, Haribabu; Takeuchi, Koh; Dubey, Abhinav; Wagner, Gerhard
• Is Part Of: Current opinion in structural biology. Volume 58(2019)
• Page Start: 294
• Page End: 304
• Publication Date: 2019-10
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2019.06.005
• Languages: English
• ISSNs: 0959-440X

Abstract

Graphical abstract: Highlights: NMR yields quantitative data on the dynamics of solution-state protein structures. NMR's impact is enhanced by continuous innovation in assignment techniques. Improvements in hardware and experimental design have extended the reach of NMR. NMR provides access to lowly populated invisible states. Information provided by NMR is unique and complements other biophysical techniques. Abstract : The first recognition of protein breathing was more than 50 years ago. Today, we are able to detect the multitude of interaction modes, structural polymorphisms, and binding-induced changes in protein structure that direct function. Solution-state NMR spectroscopy has proved to be a powerful technique, not only to obtain high-resolution structures of proteins, but also to provide unique insights into the functional dynamics of proteins. Here, we summarize recent technical landmarks in solution NMR that have enabled characterization of key biological macromolecular systems. These methods have been fundamental to atomic resolution structure determination and quantitative analysis of dynamics over a wide range of time scales by NMR. The ability of NMR to detect lowly populated protein conformations and transiently formed complexes plays a critical role in its ability to elucidate functionally important structural features of proteins and their dynamics.