Designing disorder: Tales of the unexpected tails

Intrinsically Disordered Proteins
David P MindeSander Tans

Abstract

Protein tags of various sizes and shapes catalyze progress in biosciences. Well-folded tags can serve to solubilize proteins. Small, unfolded, peptide-like tags have become invaluable tools for protein purification as well as protein-protein interaction studies. Intrinsically Disordered Proteins (IDPs), which lack unique 3D structures, received exponentially increasing attention during the last decade. Recently, large ID tags have been developed to solubilize proteins and to engineer the pharmacological properties of protein and peptide pharmaceuticals. Here, we contrast the complementary benefits and applications of both folded and ID tags based on predictions of ID. Less structure often means more function in a shorter tag.

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Citations

Nov 7, 2017·Molecular BioSystems·Harshavardhan KhareSuryanarayanarao Ramakumar
Feb 2, 2017·Proteomics·David-Paul MindeKathryn S Lilley
Aug 11, 2019·International Journal of Molecular Sciences·André F FaustinoIvo C Martins
Mar 18, 2016·Scientific Reports·Elrashdy M RedwanVladimir N Uversky
Aug 23, 2020·International Journal of Molecular Sciences·Jaime SantosSalvador Ventura
Mar 17, 2015·Intrinsically Disordered Proteins·Vladimir N Uversky
Jun 27, 2019·International Journal of Molecular Sciences·Sara SignorelliAnna Rita Bizzarri
Sep 2, 2020·International Journal of Molecular Sciences·Greta BianchiStefania Brocca

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Methods Mentioned

BETA
X-ray
optical
protein folding
pull-downs
immunoprecipitations
co-immunoprecipitation
optical tweezer
NMR
affinity purifications
SANS

Software Mentioned

PONDR

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