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How Aberrant N-Glycosylation Can Alter Protein Functionality and Ligand Binding: an Atomistic View

How Aberrant N-Glycosylation Can Alter Protein Functionality and Ligand Binding: an Atomistic View

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2756849363

How Aberrant N-Glycosylation Can Alter Protein Functionality and Ligand Binding: an Atomistic View

About this item

Full title

How Aberrant N-Glycosylation Can Alter Protein Functionality and Ligand Binding: an Atomistic View

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2022-12

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

More information

Scope and Contents

Contents

Protein assembly defects due to enrichment of aberrant conformational variants of proteins are emerging as a new frontier in therapeutics design. Understanding, atomistically, structural elements that remodel the energy landscape of proteins, with the consequence of rewiring the conformational dynamics of proteins and pathologically perturbing func...

Alternative Titles

Full title

How Aberrant N-Glycosylation Can Alter Protein Functionality and Ligand Binding: an Atomistic View

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2756849363

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2756849363

Other Identifiers

E-ISSN

2692-8205

DOI

10.1101/2022.12.22.521543