title: Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation.
abstract: Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein motions in solution could contribute to the function of proteins, even if no significant structural difference is observed in crystal structure of different states while they function. In this review, we introduce our recent report on the stabilization mechanism of human leukocyte antigen, and the possibility of fluctuation contributing to several biophysical properties of proteins.
authors: Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Tokyo 108-8639, Japan.
authors: Saeko
authors: S
authors: Yanaka
authors: Center for AIDS Research, Kumamoto University, Kumamoto 860-0811, Japan; International Research Center for Medical Sciences (IRCMS), Kumamoto University, Kumamoto 860-0811, Japan.
authors: Takamasa
authors: T
authors: Ueno
authors: Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Tokyo 108-8639, Japan; Department of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo 108-8639, Japan; Medical Proteomics Laboratory, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan.
authors: Kouhei
authors: K
authors: Tsumoto
authors: Bioorganic Research Institute, Suntory Foundation for Life Sciences, Osaka, 618-8503, Japan.
authors: Kenji
authors: K
authors: Sugase
keywords: Major Histocompatibility Complex (MHC); NMR; protein dynamics; protein stability; thermodynamics