Computational studies on protein allostery
Pr Takahisa YAMATO
Nagoya University, Japon
mercredi 21 mars 2018 - 10h00
- Salle de réunion 4004, IGBMC
Invité(e) par Biologie structurale intégrative, Roland STOTE
Within thermally fluctuating protein molecules under physiological conditions, constituent amino acid residues are tightly packed in space, having interactions with each other. Interplay between amino acid residues is one of the keys to understand protein functions at the molecular level. By using biophysical computations, we calculate inter-residue energy flow to locate strongly interacting pair of residues and identify vibrational energy transfer pathways/networks in proteins [1, 2, 3]. With this approach, we have studied the photosignal transduction mechanism of photoactive yellow protein (PYP) [4, 5], allosteric properties of proteins including PDZ domains  and hemoglobins [1, 6].
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 T. Yamato, T. Ishikura, K. Ota, T. Sakai, CURP (CURrent calculation for Proteins) version 1.1, http://www.comp-biophys.com/yamato-lab/curp.html, June 30, (2017).
 T. Ishikura, T. Yamato, Chem. Phys. Lett. 432, 533 (2006).
 T. Yamato, Energy flow pathways in photoreceptor proteins. Proteins: Energy, Heat, and Signal Flow. Eds. D. Leitner, and J. Straub, Taylor and Francis/CRC Press, pp.129–147 (2009).
 D. Leitner, J. Phys. Chem. B 120, 4019 (2016).