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- Sasaki Takanori; Razak Nur Wahida Abdul; Kato Noritaka; Mukai Yuri
- Biochemistry 2012 v.51 no.13 pp. 2785-2794
- Escherichia coli; binding capacity; cell membranes; chemical interactions; crosslinking; detergents; dissociation; gel chromatography; glutaraldehyde; heat treatment; hydroxylamine; lighting; lipids; membrane proteins; mutants; polyacrylamide gel electrophoresis; protein subunits; sodium chloride; solubilization
- ... Halorhodopsin is a retinal protein with a seven-transmembrane helix and acts as an inward light-driven Cl– pump. In this study, structural state of the solubilized halorhodopsin (NpHR) from the biomembrane of mutant strain KM-1 of Natronomonas pharaonis in nonionic detergent was investigated. A gel filtration chromatography monitored absorbances at 280 and 504 nm corresponding to the protein and a ...
- Lingyun Qin; Huili Liu; Rong Chen; Jingjing Zhou; Xiyao Cheng; Yao Chen; Yongqi Huang; Zhengding Su
- Biochemistry 2017 v.56 no.44 pp. 5943-5954
- amino acid sequences; binding capacity; chemical interactions; drugs; engineering; ligands; mice; models; molecular dynamics; mutants; oncogene proteins; pharmacology; prediction; protein conformation; protein engineering; screening
- ... The oncoprotein MdmX (mouse double minute X) is highly homologous to Mdm2 (mouse double minute 2) in terms of their amino acid sequences and three-dimensional conformations, but Mdm2 inhibitors exhibit very weak affinity for MdmX, providing an excellent model for exploring how protein conformation distinguishes and alters inhibitor binding. The intrinsic conformation flexibility of proteins plays ...