Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
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Publisher
London: Nature Publishing Group UK
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Language
English
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London: Nature Publishing Group UK
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Contents
Peptide backbone α-
N
-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides. Borosin natural product pathways are the only known ribosomally encoded and posttranslationally modified peptides (RiPPs) pathway...
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Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
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TN_cdi_doaj_primary_oai_doaj_org_article_09ca9420fa074e35a3fbd77a88dcba46
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_09ca9420fa074e35a3fbd77a88dcba46
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-021-25575-7
