Kinetic studies on subunit exchange in alpha-crystallin under external stress
Alpha-crystallin, which is the major protein in the eye lens, exists as huge molecule consisting of approximately 40 subunits and comprised of two highly homologue: alpha-A and alpha-B. Most interesting feature in alpha-crystallin is its chaperone activity, preventing the aggregation of various target proteins under external stresses such as heat and UV. One of the proposed ideas for the mechanism of its chaperone activity of alpha-crystallin is the hybridization of alpha-crystallin with target proteins and it was also found that reorganization of quaternary structure of alpha-crystallin was essential for realizing complexation. Hence it is strongly expected that subunit exchange between alpha-A and alpha-B crystallin in alpha-crystallin must be an elementary step for commencing the reorganization of quaternary structure, leading to onset its chaperone activity. We then try to study the subunit exchange between alpha-A and alpha-B crystallin under external stress:UV irradiation and heat to unveil the mechanism of its chaperone activity.
Please note that you will need to login with your ILL credentials to download the data.
Download DataThe recommended format for citing this dataset in a research publication is in the following format:
INOUE Rintaro; MARTEL Anne; OBA Yojiro; PORCAR Lionel and Masaaki Sugiyama. (2015). Kinetic studies on subunit exchange in alpha-crystallin under external stress. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-854
ILL has partnered with DataCite as the registration agency
for data persistent identifiers.