The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRSapm) is a monomer in solution

Article ID	Journal	Published Year	Pages	File Type
10870959	FEBS Letters	2013	10 Pages	PDF

Abstract

âº Tyrosyl-tRNA synthetase of mimivirus (TyrRSapm) forms weak dimers in solution. âº N-terminal TyrRSapm (ÎTyrRSapm) of mimivirus exists as a monomer in solution. âº The ligand-binding affinity for l-Tyr and ATP is not affected in ÎTyrRSapm, but is decreased 40-fold for tRNATyr.

Keywords

SDS DTT DTNB tRNA GdnHCl 5,5′-dithio-bis(2-nitrobenzoic acid)AUC amino acid Dissociation constant circular dichroism Analytical ultracentrifuge sodium dodecyl sulphate Monomer Guanidine hydrochloride