Site-Specific Isotope Labeling of FliG for Studying Structural Dynamics Using Nuclear Magnetic Resonance Spectroscopy

Tatsuro Nishikino; Yohei Miyanoiri

doi:10.1007/978-1-0716-3060-0_6

Site-Specific Isotope Labeling of FliG for Studying Structural Dynamics Using Nuclear Magnetic Resonance Spectroscopy

Methods Mol Biol. 2023:2646:57-70. doi: 10.1007/978-1-0716-3060-0_6.

Authors

Tatsuro Nishikino¹, Yohei Miyanoiri²

Affiliations

¹ Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
² Institute for Protein Research, Osaka University, Suita, Osaka, Japan. y-miyanoiri@protein.osaka-u.ac.jp.

PMID: 36842106
DOI: 10.1007/978-1-0716-3060-0_6

Abstract

To understand flagella-driven motility of bacteria, it is important to understand the structure and dynamics of the flagellar motor machinery. We have conducted structural dynamics analyses using solution nuclear magnetic resonance (NMR) to elucidate the detailed functions of flagellar motor proteins. Here, we introduce the analysis of the FliG protein, which is a flagellar motor protein, focusing on the preparation method of the original stable isotope-labeled protein.

Keywords: NMR; SAIL amino acids; Stable isotope labeling; TROSY.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins* / metabolism
Flagella* / metabolism
Isotope Labeling
Magnetic Resonance Spectroscopy
Nuclear Magnetic Resonance, Biomolecular / methods

Substances

Bacterial Proteins