Deadline of the application: September 29th (Fri), 2017
【Inquiry on the position】
Akira Shinohara, Professor, chairman of the selection committee
E-mail: ashino[at]protein.osaka-u.ac.jp (change [at] to@)
A paper”Accurate Prediction of Complex Structure and Affinity for a Flexible Protein Receptor and its Inhibitor (http://pubs.acs.org/doi/abs/10.1021/acs.jctc.6b01127, DOI: 10.1021/acs.jctc.6b01127) by Dr. Gert-Jan Bekker, who is a Specially Appointed Assistant Professor in IPR, has been published from Journal of Chemical Theory and Computation (JCTC, IF=5.301) with its cover picture of the Issue 7, 2017.
Protein Data Bank Japan (PDBj), Institute for Protein Research, Osaka University has launched the JBI (Japan alliance for Bioscience Information) portal site in collaboration with National Bioscience Database Center (NBDC), JST; Database Center for Life Science (DBCLS), Joint Support-Center for Data Science Research, ROIS; and DNA Data Bank of Japan (DDBJ), National Institute of Genetics, ROIS. This portal site provides one-stop service of databases and tools which are helpful in various scenes of the life science research.
Visit the website (http://jbioinfo.jp/) for more detail.
Deadline of the application: June 30th (Thursday), 2017
【Inquiry on the position】
Yoshie Harada, Professor, chairman of the selection committee
E-mail: yharada[at]protein.osaka-u.ac.jp (change [at] to @)
National Synchrotron Radiation Research Center (NSRRC) in Taiwan and IPR have been collaborating on the field of structure biology using synchrotron radiation for more than 10 years.
A paper about the PDBj activities in our Institute has been published in Nucleic Acids Research:
“Protein Data Bank Japan (PDBj): updated user interfaces, resource description framework, analysis tools for large structures”
A group of researchers reports on the structure and function of a novel protein named “Calredoxin”. Calredoxin binds calcium and catalyzes in dependence of its binding, redox reactions, particularly driving the detoxification of harmful oxygen species. The researchers are exploring how this protein functions at the crossroad of calcium- and redox-dependent reactions to promote efficient oxygenic photosynthesis.
A chromosome is composed of structurally and functionally distinct domains. However, the molecular mechanisms underlying the formation of chromatin structure and the function of subtelomeres, the telomere-adjacent regions, remain obscure. Here we report the roles of the conserved centromeric protein Shugoshin 2 (Sgo2) in defining chromatin structure and functions of the subtelomeres in the fission yeast Schizosaccharomyces pombe.
・Magic-angle spinning (MAS) NMR probe system with a closed-loop helium recirculation.
・Stable MAS for weeks at sample temperature T = 35 K without consuming helium.
・Multi-dimensional MAS NMR at T = 35 K at a low running cost for electricity 16 kW/h.
・An order of magnitude sensitivity gain at T = 40 K and B0 = 16.4 T.
5-Methylcytosine (5mC) is oxidized by ten-eleven translocation (TET) enzymes. This process followed by thymine DNA glycosylase is proposed to be the mechanism for methylcytosine demethylation. 5-Hydroxymethylcytosine (5hmC) is one of the most important key oxidative metabolites in the demethylation process, and therefore, simple and accurate method to determine 5hmC at single base resolution is desired. In the present study, we developed a mild catalytic oxidation of 5-hmC using micelle incarcerated oxidants that enables to determine the position of 5hmC at single base resolution.