Nucleotide Binding Modes in a Motor Protein Revealed by ³¹ P- and ¹ H-Detected MAS Solid-State NMR Spectroscopy.

ABSTRACT: Protein-nucleic acid interactions play important roles not only in energy-providing reactions, such as ATP hydrolysis, but also in reading, extending, packaging, or repairing genomes. Although they can often be analyzed in detail with X-ray crystallography, complementary methods are needed to visualize them in complexes, which are not crystalline. Here, we show how solid-state NMR spectroscopy can detect and classify protein-nucleic interactions through site-specific ¹ H- and ³¹ P-detected spectroscopic methods. The sensitivity of ¹ H chemical-shift values on noncovalent interactions involved in these molecular recognition processes is exploited allowing us to probe directly the chemical bonding state, an information, which is not directly accessible from a

SUBMITTER: Wiegand T 

PROVIDER: S-EPMC7318265 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature