title: Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
abstract: Here we describe how a (19)F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with X-ray crystallography, the quantitative comparison of the protein's dynamics in live cells and in vitro is presented. These results clearly demonstrated the greater conformational fluctuations of the intracellular protein, partially due to macromolecular crowding effects.
authors: Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Kyoto, Japan.
authors: Yousuke
authors: Y
authors: Takaoka
authors: Yoshiyuki
authors: Y
authors: Kioi
authors: Akira
authors: A
authors: Morito
authors: Junji
authors: J
authors: Otani
authors: Kyohei
authors: K
authors: Arita
authors: Eishi
authors: E
authors: Ashihara
authors: Mariko
authors: M
authors: Ariyoshi
authors: Hidehito
authors: H
authors: Tochio
authors: Masahiro
authors: M
authors: Shirakawa
authors: Itaru
authors: I
authors: Hamachi
mesh_terms: D024401:Carbonic Anhydrase I / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D004912:Erythrocytes / Q000378:metabolism*; D005462:Fluorine Radioisotopes; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013449:Sulfonamides / Q000378:metabolism; D000096926:Benzenesulfonamides
chemical_list: D024401:Carbonic Anhydrase I; D005462:Fluorine Radioisotopes; D006454:Hemoglobins; D008024:Ligands; D011506:Proteins; D013449:Sulfonamides; D000096926:Benzenesulfonamides