Binding Thermodynamics to Intrinsically Disordered Protein Domains

2020 ◽  
pp. 449-462
Author(s):  
Arne Schön ◽  
Ernesto Freire
Keyword(s):  
Protein Domains ◽  
Intrinsically Disordered Protein ◽  
Binding Thermodynamics ◽  
Intrinsically Disordered ◽  
Disordered Protein

scholarly journals PhosIDP: a web tool to visualize the location of phosphorylation sites in disordered regions

2021 ◽  
Author(s):  
Sonia T. Nicolaou ◽  
Max Hebditch ◽  
Owen J. Jonathan ◽  
Chandra S. Verma ◽  
Jim Warwicker
Keyword(s):  
Protein Domains ◽  
Intrinsically Disordered Protein ◽  
Phosphorylation Sites ◽  
Web Tool ◽  
Functional Interpretation ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Intrinsically Disordered Region ◽  
Condensate Formation ◽  
The Web

AbstractCharge is a key determinant of intrinsically disordered protein (IDP) and intrinsically disordered region (IDR) properties. IDPs and IDRs are enriched in sites of phosphorylation, which alters charge. Visualizing the degree to which phosphorylation modulates the charge profile of a sequence would assist in the functional interpretation of IDPs and IDRs. PhosIDP is a web tool that shows variation of charge and fold propensity upon phosphorylation. In combination with the displayed location of protein domains, the information provided by the web tool can lead to functional inferences for the consequences of phosphorylation. IDRs are components of many proteins that form biological condensates. It is shown that IDR charge, and its modulation by phosphorylation, is more tightly controlled for proteins that are essential for condensate formation than for those present in condensates but inessential.

scholarly journals Fast Association and Slow Transitions in the Interaction between Two Intrinsically Disordered Protein Domains

2012 ◽  
Vol 287 (41) ◽  
pp. 34316-34324 ◽  
Author(s):  
Jakob Dogan ◽  
Tanja Schmidt ◽  
Xin Mu ◽  
Åke Engström ◽  
Per Jemth
Keyword(s):  
Protein Domains ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein

Acceleration of an Enzymatic Reaction in Liquid Phase Separated Compartments Based on Intrinsically Disordered Protein Domains

2020 ◽  
Vol 2 (4) ◽  
Author(s):  
Andreas M. Küffner ◽  
Marc Prodan ◽  
Remo Zuccarini ◽  
Umberto Capasso Palmiero ◽  
Lenka Faltova ◽  
...  
Keyword(s):  
Liquid Phase ◽  
Enzymatic Reaction ◽  
Protein Domains ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein

Acceleration of an Enzymatic Reaction in Liquid Phase Separated Compartments Based on Intrinsically Disordered Protein Domains

2020 ◽  
Vol 2 (4) ◽  
Author(s):  
Andreas M. Küffner ◽  
Marc Prodan ◽  
Remo Zuccarini ◽  
Umberto Capasso Palmiero ◽  
Lenka Faltova ◽  
...  
Keyword(s):  
Liquid Phase ◽  
Enzymatic Reaction ◽  
Protein Domains ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein

scholarly journals PhosIDP: a web tool to visualize the location of phosphorylation sites in disordered regions

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sonia T. Nicolaou ◽  
Max Hebditch ◽  
Owen J. Jonathan ◽  
Chandra S. Verma ◽  
Jim Warwicker
Keyword(s):  
Protein Domains ◽  
Intrinsically Disordered Protein ◽  
Phosphorylation Sites ◽  
Web Tool ◽  
Functional Interpretation ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Intrinsically Disordered Region ◽  
Condensate Formation ◽  
The Web

AbstractCharge is a key determinant of intrinsically disordered protein (IDP) and intrinsically disordered region (IDR) properties. IDPs and IDRs are enriched in sites of phosphorylation, which alters charge. Visualizing the degree to which phosphorylation modulates the charge profile of a sequence would assist in the functional interpretation of IDPs and IDRs. PhosIDP is a web tool that shows variation of charge and fold propensity upon phosphorylation. In combination with the displayed location of protein domains, the information provided by the web tool can lead to functional inferences for the consequences of phosphorylation. IDRs are components of many proteins that form biological condensates. It is shown that IDR charge, and its modulation by phosphorylation, is more tightly controlled for proteins that are essential for condensate formation than for those present in condensates but inessential.

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