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• W1972178744 abstract "Abstract N -linked glycosylation is one of the most important, chemically complex and ubiquitous post-translational modifications in all eukaryotes. The N -glycans that are covalently linked to proteins are involved in numerous biological processes. There is considerable interest in developments of general approaches to predict the structural consequences of site-specific glycosylation and to understand how these effects can be exploited in protein design with advantageous properties. In this study, the impacts of N -glycans on protein structure and dynamics are systematically investigated using an integrated computational approach of the Protein Data Bank structure analysis and atomistic molecular dynamics simulations of glycosylated and deglycosylated proteins. Our study reveals that N -glycosylation does not induce significant changes in protein structure, but decreases protein dynamics, likely leading to an increase in protein stability. Overall, these results suggest not only a common role of glycosylation in proteins, but also a need for certain proteins to be properly glycosylated to gain their intrinsic dynamic properties." @default.
• W1972178744 created "2016-06-24" @default.
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• W1972178744 date "2015-03-09" @default.
• W1972178744 modified "2023-10-14" @default.
• W1972178744 title "Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study" @default.
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• W1972178744 doi "https://doi.org/10.1038/srep08926" @default.
• W1972178744 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4352867" @default.
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