Beta-amyloid Peptides, N. S. Lam, M. Kouza, H. Zung, M. S. Li, ...
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Kouza, Maksim, Hu, Chin-Kun, Li, Mai Suan
We have developed a new extended replica exchange method to study thermodynamics of a system in the presence of external force. Our idea is based on the exchange between different force replicas to...
Effect of finite size on cooperativity and rates of protein folding (2006)
Kouza, Maksim, Li, Mai Suan, O'Brien Jr., Edward P., Hu, Chin-Kun, Thirumalai, D.
We analyze the dependence of cooperativity of the thermal denaturation transition and folding rates of globular proteins on the number of amino acid residues, $N$, using lattice models with side...
Folding of the Protein Domain hbSBD (2006)
Kouza, Maksim, Chang, Chi-Fon, Hayryan, Shura, Yu, Tsan-hung, Li, Mai Suan, Huang, Tai-huang, ...
The folding of the alpha-helice domain hbSBD of the mammalian mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex is studied by the circular dichroism technique in absence of...
Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin (2006)
Li, Mai Suan, Kouza, Maksim, Hu, Chin-Kun
The refolding from stretched initial conformations of ubiquitin (PDB ID: 1ubq) under the quenched force is studied using the Go model and the Langevin dynamics. It is shown that the refolding...
Folding of the Protein Domain hbSBD
Kouza, Maksim, Chang, Chi-Fon, Hayryan, Shura, Yu, Tsan-hung, Li, Mai Suan, Huang, Tai-huang, ...
The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal...
Folding of the Protein Domain hbSBD
Kouza, Maksim, Chang, Chi-Fon, Hayryan, Shura, Yu, Tsan-hung, Li, Mai Suan, Huang, Tai-huang, ...
The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal...
Refolding upon Force Quench and Pathways of Mechanical and Thermal Unfolding of Ubiquitin
Li, Mai Suan, Kouza, Maksim, Hu, Chin-Kun
The refolding from stretched initial conformations of ubiquitin (PDB ID: 1ubq) under the quenched force is studied using the Cα-Gō model and the Langevin dynamics. It is shown that the refolding...