the stability and formation of native proteins from unfolded monomers is increased through interactions with unrelated proteins从展开的稳定和形成原生蛋白质单体通过相互作用增加不相关的蛋白质.pdfVIP

The Stability and Formation of Native Proteins from Unfolded Monomers Is Increased through Interactions with Unrelated Proteins ´ ´ 1 2 2 ´ 1 ´ 1 ´ Claudia Rodrıguez-Almazan , Francisco J. Torner , Miguel Costas , Ruy Perez-Montfort , Marieta Tuena de Gomez-Puyou , Armando Gomez Puyou1* ´ ´ ´ ´ 1 Departamento de Bioquımica, Instituto de Fisiologıa Celular, Universidad Nacional Autonoma de Mexico, Mexico City, Mexico, 2 Laboratorio de ´ ´ ´ ´ ´ Biofisicoquımica, Departamento de Fisicoquımica, Facultad de Quımica, Universidad Nacional Autonoma de Mexico, Mexico City, Mexico The intracellular concentration of protein may be as high as 400 mg per ml; thus it seems inevitable that within the cell, numerous protein-protein contacts are constantly occurring. A basic biochemical principle states that the equilibrium of an association reaction can be shifted by ligand binding. This indicates that if within the cell many protein-protein interactions are indeed taking place, some fundamental characteristics of proteins would necessarily differ from those observed in traditional biochemical systems. Accordingly, we measured the effect of eight different proteins on the formation of homodimeric triosephosphate isomerase from Trypanosoma brucei (TbTIM) from guanidinium chloride unfolded monomers. The eight proteins at concentrations of micrograms per ml induced an important increase on active dimer formation. Studies on the mechanism of this phenomenon showed that the proteins stabilize the dim