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Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
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| Title: | Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive |
| Authors: | Mahatabuddin, Sheikh Browse this author | | Hanada, Yuichi Browse this author | | Nishimiya, Yoshiyuki Browse this author | | Miura, Ai Browse this author | | Kondo, Hidemasa Browse this author | | Davies, Peter L. Browse this author | | Tsuda, Sakae Browse this author →KAKEN DB |
| Issue Date: | 13-Feb-2017 |
| Publisher: | Nature Publishing Group |
| Journal Title: | Scientific reports |
| Volume: | 7 |
| Start Page: | 42501 |
| Publisher DOI: | 10.1038/srep42501 |
| Abstract: | A supersoluble 40-residue type I antifreeze protein (AFP) was discovered in a righteye flounder, the barfin plaice (bp). Unlike all other AFPs characterized to date, bpAFP transitions from moderately-active to hyperactive with increasing concentration. At sub-mM concentrations, bpAFP bound to pyramidal planes of ice to shape it into a bi-pyramidal hexagonal trapezohedron, similarly to the other moderately-active AFPs. At sub-mM concentrations, bpAFP uniquely underwent further binding to the whole ice crystal surface including the basal planes. The latter caused a bursting ice crystal growth normal to c-axis, 3 degrees C of high thermal hysteresis, and alteration of an ice crystal into a smaller lemon-shaped morphology, all of which are well-known properties of hyperactive AFPs. Analytical ultracentrifugation showed this activity transition is associated with oligomerization to form tetramer, which might be the forerunner of a naturally occurring four-helix-bundle AFP in other flounders. |
| Rights: | https://creativecommons.org/licenses/by/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/65433 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 津田 栄
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