scholarly journals A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy

2019 ◽  
Vol 141 (44) ◽  
pp. 17817-17829 ◽  
Author(s):  
Wiktor Adamski ◽  
Nicola Salvi ◽  
Damien Maurin ◽  
Justine Magnat ◽  
Sigrid Milles ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Protein Dynamics ◽  
Intrinsically Disordered Protein ◽  
Physiological Conditions ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Unified Description

scholarly journals Intrinsically Disordered Protein Dynamics Uncovered through Dynamic Flexibility Index (DFI) Analysis

2017 ◽  
Vol 112 (3) ◽  
pp. 208a-209a
Author(s):  
Tushar Modi ◽  
Gül H. Zerze ◽  
Jeetain Mittal ◽  
Sara M. Vaiana ◽  
S. Banu Ozkan
Keyword(s):  
Protein Dynamics ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Flexibility Index

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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