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Glycine Rich Segments Adopt Polyproline II Helices Which May Contribute to Biomolecular Condensate F...

Glycine Rich Segments Adopt Polyproline II Helices Which May Contribute to Biomolecular Condensate F...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_biorxiv_primary_2020_07_30_229062

Glycine Rich Segments Adopt Polyproline II Helices Which May Contribute to Biomolecular Condensate Formation

About this item

Full title

Glycine Rich Segments Adopt Polyproline II Helices Which May Contribute to Biomolecular Condensate Formation

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2020-07

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

More information

Scope and Contents

Contents

Many intrinsically disordered proteins contain Gly-rich regions which are generally assumed to be disordered. Such regions often form biomolecular condensates which play essential roles in organizing cellular processes. However, the bases of their formation and stability are still not completely understood. Considering NMR studies of the Gly-rich H...

Alternative Titles

Full title

Glycine Rich Segments Adopt Polyproline II Helices Which May Contribute to Biomolecular Condensate Formation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_biorxiv_primary_2020_07_30_229062

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_biorxiv_primary_2020_07_30_229062

Other Identifiers

ISSN

2692-8205

E-ISSN

2692-8205

DOI

10.1101/2020.07.30.229062

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