![]() ![]() RIKEN Genomic Sciences Center, Yokohama, Japan. Analyses of 1H-15N heteronuclear single quantum correlation spectra revealed that a wide range of residues in the C-terminal region, as well as the residues in the vicinity of a hydrophobic patch in the N-terminal domain, were dramatically affected upon complex formation with ribosomal protein S19. On the other hand, the C-terminal region of RimM (residues 81 to 162) is partly folded in solution. ![]() Residues 1 to 80 of the RimM protein fold into a single structural domain adopting a six-stranded beta-barrel fold. In the present study, we have produced Thermus thermophilus RimM in both the full-length form (162 residues) and its N-terminal fragment, spanning residues 1 to 85, as soluble proteins in Escherichia coli and have performed structural analyses by nuclear magnetic resonance spectroscopy. 834 animal species have been identified by scientists in Lot-et-Garonne, including 219 that are threatened, such as the European eel, the skylark, the greylag. Multiple sequence alignments predicted that RimM possesses two domains in its N- and C-terminal regions. It binds to ribosomal protein S19, located in the head domain of the 30S subunit. The RimM protein has been implicated in the maturation of the 30S ribosomal subunit.
0 Comments
Leave a Reply. |
Details
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |