Protein structure and its folding rate
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Publication:4607148
DOI10.1007/978-3-540-76784-8_9zbMATH Open1382.92208OpenAlexW96373505MaRDI QIDQ4607148FDOQ4607148
Authors: Alexei V. Finkelstein, Dmitry N. Ivankov, Sergiy O. Garbuzynskiy, Oxana V. Galzitskaya 
Publication date: 12 March 2018
Published in: Applied Optimization (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/978-3-540-76784-8_9
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Cited In (18)
- Protein's native state stability in a chemically induced denaturation mechanism
- Equilibrium protein folding-unfolding process involving multiple intermediates
- Protein folding disorders: toward a basic biological paradigm
- The local topological free energy of proteins
- Size scaling behaviour in protein domains belonging to the all-\(\alpha \), all-\(\beta \), \(\alpha / \beta \), and \(\alpha + \beta \) folding classes
- Protein model exhibiting three folding transitions
- Scaling laws in simple and complex proteins: Size scaling effects associated with domain number and folding class
- Mathematics of protein pathological misfolding
- A novel procedure for identification of the folding/unfolding patterns of dimeric proteins
- Protein sequence and structure: is one more fundamental than the other?
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- Out-of-equilibrium versus dynamical and thermodynamical transitions for a model protein
- Protein folding: a good structure protector is also a good structure seeker
- Statistical mechanical theory of protein folding in water environment
- Influence of conformational entropy on the protein folding rate
- Thermodynamics of proteins: Fast folders and sharp transitions
- Structural susceptibilities in toy models of proteins
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