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- W3138045007 abstract "N-linked glycans are ubiquitous in nature and play key roles in biology. For example, glycosylation of pathogenic proteins is a common immune evasive mechanism, hampering the development of successful vaccines. Due to their chemical variability and complex dynamics, an accurate molecular understanding of glycans is still limited by the lack of effective resolution of current experimental approaches. Here, we have developed and implemented a reductive model based on the popular Martini 2.2 coarse-grained force field for the computational study of N-glycosylation. We used the HIV-1 Env as a direct applied example of a highly glycosylated protein. Our results indicate that the model not only reproduces many observables in very good agreement with a fully atomistic force field but also can be extended to study large amount of glycosylation variants, a fundamental property that can aid in the development of drugs and vaccines." @default.
- W3138045007 created "2021-03-29" @default.
- W3138045007 creator A5063460625 @default.
- W3138045007 creator A5071669681 @default.
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- W3138045007 creator A5090001717 @default.
- W3138045007 date "2021-03-20" @default.
- W3138045007 modified "2023-10-17" @default.
- W3138045007 title "Development of Martini 2.2 parameters for <i>N</i>-glycans: a case study of the HIV-1 Env glycoprotein dynamics" @default.
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- W3138045007 doi "https://doi.org/10.1093/glycob/cwab017" @default.
- W3138045007 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8351497" @default.
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- W3138045007 hasPublicationYear "2021" @default.
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