Thermodynamic Aspects of Coupled Binding and Folding of an Intrinsically Disordered Protein: A Computational Alanine Scanning Study

Biochemistry ◽  
2009 ◽  
Vol 48 (48) ◽  
pp. 11332-11334 ◽  
Author(s):  
L. Michel Espinoza-Fonseca
Keyword(s):  
Protein A ◽  
Intrinsically Disordered Protein ◽  
Alanine Scanning ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Computational Alanine Scanning

scholarly journals Intrinsically Disordered Protein: A Thermodynamic Perspective

2015 ◽  
Vol 108 (2) ◽  
pp. 228a
Author(s):  
Jing Li ◽  
James O. Wrabl ◽  
Vincent J. Hilser
Keyword(s):  
Protein A ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

2018 ◽  
Author(s):  
Sarah Klass ◽  
Matthew J. Smith ◽  
Tahoe Fiala ◽  
Jessica Lee ◽  
Anthony Omole ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Fusion Proteins ◽  
Organic Molecules ◽  
Intrinsically Disordered Protein ◽  
Protein Domain ◽  
Enzymatic Cleavage ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Self Assembling ◽  
Protein Tag

Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on a human intrinsically disordered protein, which has been appended with a hydrophobic segment. The micelles were found to form across a broad range of pH, ionic strength, and temperature conditions, with critical micelle concentration (CMC) values below 1 µM being observed in some cases. The reported micelles were found to solubilize hydrophobic metal complexes and organic molecules, suggesting their potential suitability for catalysis and drug delivery applications.

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