Replica exchange molecular dynamics simulation study on the mechanism of desiccation-induced structuralization of an intrinsically disordered peptide as a model of LEA proteins
Group 3 late embryogenesis abundant (G3LEA) proteins, which act as a well-characterized desiccation protectant in anhydrobiotic organisms, are structurally disordered in solution, but they acquire a predominantly α-helical structure during drying. Thus, G3LEA proteins are now accepted as intrinsical...
Main Authors: | Tatsushi Nishimoto, Yuta Takahashi, Shohei Miyama, Tadaomi Furuta, Minoru Sakurai |
---|---|
Format: | Article |
Language: | English |
Published: |
The Biophysical Society of Japan
2019-11-01
|
Series: | Biophysics and Physicobiology |
Subjects: | |
Online Access: | https://doi.org/10.2142/biophysico.16.0_196 |
Similar Items
-
Structural Plasticity of Intrinsically Disordered LEA Proteins from Xerophyta schlechteri Provides Protection In Vitro and In Vivo
by: Mariana A. Silva Artur, et al.
Published: (2019-10-01) -
Pleiotropic roles of late embryogenesis abundant proteins of Deinococcus radiodurans against oxidation and desiccation
by: Yingying Liu, et al.
Published: (2021-01-01) -
Impact of multivalent charge presentation on peptide–nanoparticle aggregation
by: Daniel Schöne, et al.
Published: (2015-05-01) -
Late Embryogenesis Abundant Protein–Client Protein Interactions
by: Lynnette M.A. Dirk, et al.
Published: (2020-06-01) -
Decoding the Divergent Subcellular Location of Two Highly Similar Paralogous LEA Proteins
by: Marie-Hélène Avelange-Macherel, et al.
Published: (2018-05-01)