Title : Role of Disulfide Bonds and Topological Frustration in the Kinetic Partitioning of Lysozyme Folding Pathways.

Pub. Date : 2019 Apr 18

PMID : 30913878






4 Functional Relationships(s)
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1 Role of Disulfide Bonds and Topological Frustration in the Kinetic Partitioning of Lysozyme Folding Pathways. Disulfides lysozyme Homo sapiens
2 Lysozyme has four disulfide bonds and is widely studied for its antibacterial properties. Disulfides lysozyme Homo sapiens
3 Using a coarse-grained protein model and simulations, we show that two out of the four disulfide bonds, which are present in the alpha-domain of lysozyme, are responsible for the slow folding pathway. Disulfides lysozyme Homo sapiens
4 These results show that lysozyme also serves as a very good model system to probe the role of disulfide bonds and topological frustration in protein folding. Disulfides lysozyme Homo sapiens