Replica exchange molecular dynamics simulation study on the mechanism of desiccation-induced structuralization of an intrinsically disordered peptide as a model of LEA proteins

Author:

Nishimoto Tatsushi1,Takahashi Yuta1,Miyama Shohei1,Furuta Tadaomi1,Sakurai Minoru1

Affiliation:

1. Center for Biological Resources and Informatics, Tokyo Institute of Technology

Publisher

Biophysical Society of Japan

Subject

General Medicine

Reference18 articles.

1. [2] Tompa, P. Intrinsically disordered proteins: a 10-year recap. Trends Biochem. Sci. 37, 509–516 (2012).

2. [6] Goyal, K., Tisi, L., Basran, A., Browne, J., Burnell, A., Zurdo, J., et al. A. Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J. Biol. Chem. 278, 12977–12984 (2003).

3. [7] Tolleter, D., Jaquinod, M., Mangavel, C., Passirani, C., Saulnier, P., Manon, S., et al. Structure and function of a mitochondrial late embryogenesis abundant protein are revealed by desiccation. Plant Cell 19, 1580–1589 (2007).

4. [9] Hatanaka, R., Hagiwara-Komoda, Y., Furuki, T., Kanamori, Y., Fujita, M., Cornette, R., et al. An abundant LEA protein in the anhydrobiotic midge, PvLEA4, act as a molecular shield by limiting growth of aggregating protein particles. Insect Biochem. Mol. Biol. 43, 1055–1067 (2013).

5. [14] Shimizu, T., Kanamori, Y., Furuki, T., Kikawada, T., Okuda, T., Takahashi, T., et al. Desiccation-induced structuralizatoin and glass formation of group 3 late embryogenesis abundant protein model peptides. Biochemistry 49, 1093–1104 (2010).

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