α-helix formation rate of oligopeptides at subzero temperatures
Author:
Affiliation:
1. Department of Physics, Kansai Medical University
2. Department of Environmental Engineering for Symbiosis, Soka University
3. Department of Bioinformatics, Soka University
4. Present address: Hinomoto Gakuen Institute
Publisher
Biophysical Society of Japan
Subject
Biophysics
Link
https://www.jstage.jst.go.jp/article/biophysics/10/0/10_9/_pdf
Reference18 articles.
1. 1. Ballew, R. M., Sabelko, J. & Gruebele, M. Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl. Acad. Sci. USA 93, 5759-5764 (1996).
2. 2. Clarke, D. T., Doig, A. J., Stapley, B. J. & Jones, G. R. The alpha-helix folds on the millisecond time scale. Proc. Natl. Acad. Sci. USA 96, 7232-7237 (1999).
3. 3. Qin, Z-J., Hu, D-M., Shimada, L., Nakagawa, T., Arai, M., Zhou, J-M. & Kihara, H. Refolding of β-lactoglobulin studied by stopped-flow circular dichroism at subzero temperatures. FEBS Lett. 507, 299-302 (2001).
4. 4. Li, J., Shinjo, M., Matsumura, Y., Morita, M., Baker, D., Ikeguchi, M. & Kihara, H. An α-Helical Burst in the src SH3 Folding Pathway. Biochemistry 46, 5072-5082 (2007).
5. 5. Matsumura, Y., Shinjo, M., Mahajan, A., Tsai, M-D. & Kihara, H. α-Helical burst on the folding pathway of FHA domains from Rad53 and Ki67. Biochimie 92, 1031-1039 (2010).
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1. Unfolding of α-helical 20-residue poly-glutamic acid analyzed by multiple runs of canonical molecular dynamics simulations;PeerJ;2018-05-15
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