intrinsically disordered proteins Search Results


structural ensembles of intrinsically disordered proteins depend strongly on force field: a comparison to experiment  (Rauscher GmbH)
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Rauscher GmbH structural ensembles of intrinsically disordered proteins depend strongly on force field: a comparison to experiment
Structural Ensembles Of Intrinsically Disordered Proteins Depend Strongly On Force Field: A Comparison To Experiment, supplied by Rauscher GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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structural ensembles of intrinsically disordered proteins depend strongly on force field: a comparison to experiment - by Bioz Stars, 2026-07
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intrinsically disordered proteins  (InterPro Inc)
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InterPro Inc intrinsically disordered proteins
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
Intrinsically Disordered Proteins, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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intrinsically disordered proteins - by Bioz Stars, 2026-07
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intrinsically disordered proteins  (Federation of European Neuroscience Societies)
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Federation of European Neuroscience Societies intrinsically disordered proteins
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
Intrinsically Disordered Proteins, supplied by Federation of European Neuroscience Societies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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intrinsically disordered proteins - by Bioz Stars, 2026-07
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computational characterization of hybrid proteins containing ordered and intrinsically disordered regions  (CEITEC laboratories)
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CEITEC laboratories computational characterization of hybrid proteins containing ordered and intrinsically disordered regions
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
Computational Characterization Of Hybrid Proteins Containing Ordered And Intrinsically Disordered Regions, supplied by CEITEC laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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computational characterization of hybrid proteins containing ordered and intrinsically disordered regions - by Bioz Stars, 2026-07
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p.5.1-003 nmr characterization of intrinsically disordered microtubule associated protein 2c  (CEITEC laboratories)
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CEITEC laboratories p.5.1-003 nmr characterization of intrinsically disordered microtubule associated protein 2c
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
P.5.1 003 Nmr Characterization Of Intrinsically Disordered Microtubule Associated Protein 2c, supplied by CEITEC laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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p.5.1-003 nmr characterization of intrinsically disordered microtubule associated protein 2c - by Bioz Stars, 2026-07
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intrinsically disordered proteins  (CEITEC laboratories)
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CEITEC laboratories intrinsically disordered proteins
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
Intrinsically Disordered Proteins, supplied by CEITEC laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/intrinsically+disordered+proteins/pm31092000-1-10-6?v=CEITEC+laboratories
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intrinsically disordered proteins - by Bioz Stars, 2026-07
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recombinant yy1- idr (intrinsically disordered regions)–egfp fusion protein  (GenScript corporation)
90
GenScript corporation recombinant yy1- idr (intrinsically disordered regions)–egfp fusion protein
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
Recombinant Yy1 Idr (Intrinsically Disordered Regions)–Egfp Fusion Protein, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/intrinsically+disordered+proteins/pm37094986-367-5-16?v=GenScript+corporation
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recombinant yy1- idr (intrinsically disordered regions)–egfp fusion protein - by Bioz Stars, 2026-07
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and recombinant intrinsically disordered protein  (BioMimetic Therapeutics)
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BioMimetic Therapeutics and recombinant intrinsically disordered protein
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
And Recombinant Intrinsically Disordered Protein, supplied by BioMimetic Therapeutics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/intrinsically+disordered+proteins/pm27008568-119-14-10?v=BioMimetic+Therapeutics
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and recombinant intrinsically disordered protein - by Bioz Stars, 2026-07
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mini-review structural biology of intrinsically disordered proteins: revisiting unsolved mysteries  (SignaBlok Inc)
90
SignaBlok Inc mini-review structural biology of intrinsically disordered proteins: revisiting unsolved mysteries
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
Mini Review Structural Biology Of Intrinsically Disordered Proteins: Revisiting Unsolved Mysteries, supplied by SignaBlok Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mini-review structural biology of intrinsically disordered proteins: revisiting unsolved mysteries - by Bioz Stars, 2026-07
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protein intrinsic disorder and human papillomaviruses  (Molecular Kinetics Inc)
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Molecular Kinetics Inc protein intrinsic disorder and human papillomaviruses
(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically <t>disordered</t> RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).
Protein Intrinsic Disorder And Human Papillomaviruses, supplied by Molecular Kinetics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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protein intrinsic disorder and human papillomaviruses - by Bioz Stars, 2026-07
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Image Search Results


(A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically disordered RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).

Journal: Frontiers in Fungal Biology

Article Title: Cprp—An Unusual, Repetitive Protein Which Impacts Pleuromutilin Biosynthesis in the Basidiomycete Clitopilus passeckerianus

doi: 10.3389/ffunb.2021.655323

Figure Lengend Snippet: (A) Both DDR48 and Cprp are shown to be highly repetitive proteins with low amino acid sequence complexity, being enriched in asparagine, serine, aspartic acid, and glycine residues. Both contain multiple [G/S]-Y-[G/S] motifs (in red), which are known to be present in intrinsically disordered RNA-binding proteins. (B) A PLAAC analysis of Cprp and DDR48 showing regions (framed in red) which are predicted to be prion-like domains (Lancaster et al., ).

Article Snippet: Another feature that the fungal proteins share with the human RNA-binding proteins is that they are all predicted to be intrinsically disordered proteins (as analyzed by InterPro), which are characterized by a lack of defined three-dimensional structure.

Techniques: Sequencing, RNA Binding Assay