Comparison of the Conformational Stability of the Molten Globule and Native States of Horse Cytochrome c
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Cited by 168 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Effect of proline content and histidine ligation on the dynamics of Ω-loop D and the peroxidase activity of iso-1-cytochrome c;Journal of Inorganic Biochemistry;2024-03
2. Determinants for macromolecular crowding-induced thermodynamic stabilization of acid-denatured cytochrome c to molten globules;Journal of Molecular Liquids;2023-10
3. Effect on intrinsic peroxidase activity of substituting coevolved residues from Ω-loop C of human cytochrome c into yeast iso-1-cytochrome c;Journal of Inorganic Biochemistry;2022-07
4. Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A;Biochemistry;2022-04-16
5. Singlet oxygen quenching as a probe for cytochrome c molten globule state formation;Physical Chemistry Chemical Physics;2022
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