Characterization of protein folding by a Φ-value calculation with a statistical-mechanical model
Author:
Affiliation:
1. School of Social Sciences, Waseda University
2. Department of Electrical Engineering, Nishinippon Institute of Technology
Publisher
Biophysical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/biophysico/13/0/13_263/_pdf
Reference18 articles.
1. [7] Muñoz, V. A simple theoretical model goes a long way in explaining complex behavior in protein folding. Proc. Natl. Acad. Sci. USA 111, 15863–15864 (2014).
2. [8] Wako, H. & Saitô, N. Statistical mechanical theory of the protein conformation. I. General considerations and the application to homopolymers. J. Phys. Soc. Jpn. 44, 1931–1938 (1978).
3. [9] Wako, H. & Saitô, N. Statistical mechanical theory of the protein conformation. II. Folding pathway for protein. J. Phys. Soc. Jpn. 44, 1939–1945 (1978).
4. [22] Alm, E. & Baker, D. Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures. Proc. Natl. Acad. Sci. USA 96, 11305–11310 (1999).
5. [25] Itoh, K. & Sasai, M. Flexibly varying folding mechanism of a nearly symmetrical protein: B domain of protein A. Proc. Natl. Acad. Sci. USA 103, 7298–7303 (2006).
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