Prediction of α-Helix Folding of Isolated C-Peptide of Ribonuclease A by Monte Carlo Simulated Annealing
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
https://www.jstage.jst.go.jp/article/cl/20/2/20_2_213/_pdf
Reference9 articles.
1. Optimization by Simulated Annealing
2. A prediction of tertiary structures of peptide by the Monte Carlo simulated annealing method
3. The Three-Dimensional Structure of Ribonuclease-S
4. Helix-coil transition of the isolated amino terminus of ribonuclease
5. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A.
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2. A Fast Convergent Simulated Annealing Algorithm for Protein-Folding: Simulated Annealing Outlier FLOODing (SA-OFLOOD) Method;Bulletin of the Chemical Society of Japan;2016-11-15
3. Minimal Model of Intrinsic Chirality to Study the Folding Behavior of Helical Polymers;Macromolecules;2014-08-21
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5. Relaxation mode analysis of a peptide system: Comparison with principal component analysis;The Journal of Chemical Physics;2011-10-28
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