Research Project
Grant-in-Aid for Challenging Exploratory Research
Hydrophobic interactions are known to be essential for biomolecular recognition. In this project, our hypothesis that concerted bimolecular movements lead to stabilization of complexation was confirmed by experimental data. Fatty acid and fatty-acid binding proteins were subjected to the structural determination by X-ray analysis. The results clearly showed that fatty acids with an alkyl chain longer than C14 have highly flexible conformation around their terminal methyl group. These movements of alkyl chains hardly prevent high affinity of fatty acids, thus supporting that a rapid movements of ligand molecules do not always decrease bimolecular affinity but stabilize the ligand binding.
All 2014 2013 2012 Other
All Journal Article (7 results) (of which Peer Reviewed: 7 results) Presentation (14 results) Book (2 results) Remarks (2 results)
Org. Lett
Volume: 16巻 Issue: 3 Pages: 844-847
10.1021/ol4036159
Biochim. Biophys. Acta
Volume: 1838巻 Issue: 5 Pages: 1372-1381
10.1016/j.bbamem.2014.01.017
Bioorganic & Medicinal Chemistry
Volume: 22 Issue: 6 Pages: 1804-8
10.1016/j.bmc.2014.02.001
Volume: 1838 Pages: 1372-81
J. Synchrotron Rad.
Volume: 20 Issue: 6 Pages: 923-8
10.1107/s0909049513021298
Biochemistry
Volume: 51 Issue: 42 Pages: 8363-8370
10.1021/bi3009399
Bioorg. Med. Chem
Volume: 20巻 Issue: 19 Pages: 5699-5704
10.1016/j.bmc.2012.08.016
http://www.chem.sci.osaka-u.ac.jp/lab/murata/