Computational Study of the Mechanism Underlying the Anti-aggregation Function of a Group3LEA Peptide
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- YAMAKAWA Kentaro
- Center for Biological Resources and Informatics, Tokyo Institute of Technology
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- FURUKI Takao
- Center for Biological Resources and Informatics, Tokyo Institute of Technology
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- FURUTA Tadaomi
- Center for Biological Resources and Informatics, Tokyo Institute of Technology
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- SAKURAI Minoru
- Center for Biological Resources and Informatics, Tokyo Institute of Technology
Bibliographic Information
- Other Title
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- Group3LEAペプチドのタンパク質凝集抑制メカニズムに関する計算化学的研究
- Group3LEA ペプチド ノ タンパクシツ ギョウシュウ ヨクセイ メカニズム ニ カンスル ケイサン カガクテキ ケンキュウ
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Abstract
Here, we have performed molecular dynamics (MD) simulations of a short model peptide which has two tandem repeats of the 11-mer motif of a group3 late embryogenesis abundant protein in aqueous solution. First we showed that this peptide (LEA peptide) adopts turn-like structures in water with the hydrophilic side chains being exposed to the medium. Next, we performed MD simulations for the mixed system of the LEA peptide and lysozyme and showed that the LEA peptide binds to the surface of lysozyme through the intermolecular hydrogen bonds with three different binding patterns. Interestingly, the conformation of the LEA peptide is transformed into more extended form with binding to lysozyme. It is concluded that the LEA peptide could protect lysozyme from aggregation by shielding the protein surface in the dry state. In other words, the LEA peptide works as a chemical chaperon.
Journal
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- Cryobiology and Cryotechnology
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Cryobiology and Cryotechnology 59 (2), 101-105, 2013
Japanese Society of Cryobiology and Cryotechnology
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Details 詳細情報について
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- CRID
- 1390282680062517376
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- NII Article ID
- 110009662023
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- NII Book ID
- AN10448734
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- ISSN
- 24241555
- 13407902
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- NDL BIB ID
- 024984975
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed