scholarly journals Conformational Preferences of an Intrinsically Disordered Protein Domain: A Case Study for Modern Force Fields

2020 ◽  
Author(s):  
Srinivasa M. Gopal ◽  
Sebastian Wingbermühle ◽  
Jan Schnatwinkel ◽  
Selina Juber ◽  
Christian Herrmann ◽  
...  
Keyword(s):  
Force Fields ◽  
Intrinsically Disordered Protein ◽  
Protein Domain ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Conformational Preferences

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.

scholarly journals Rejuvenation Of CcdB-poisoned Gyrase By An Intrinsically Disordered Protein Domain

2009 ◽  
Vol 96 (3) ◽  
pp. 319a
Author(s):  
Natalie De Jonge ◽  
Buts Lieven ◽  
Abel Garcia-Pino ◽  
Henri De Greve ◽  
Lode Wyns ◽  
...  
Keyword(s):  
Intrinsically Disordered Protein ◽  
Protein Domain ◽  
Intrinsically Disordered ◽  
Disordered Protein

The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue

2018 ◽  
Vol 475 (14) ◽  
pp. 2271-2291 ◽  
Author(s):  
José L. Neira ◽  
María Belén López ◽  
Paz Sevilla ◽  
Bruno Rizzuti ◽  
Ana Cámara-Artigas ◽  
...  
Keyword(s):  
Hot Spot ◽  
Intrinsically Disordered Protein ◽  
Prothymosin Α ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Conformational Preferences ◽  
Folded Proteins ◽  
Similar Affinity ◽  
Polycomb Complex ◽  
Micromolar Range

NUPR1 is a protumoral multifunctional intrinsically disordered protein (IDP), which is activated during the acute phases of pancreatitis. It interacts with other IDPs such as prothymosin α, as well as with folded proteins such as the C-terminal region of RING1-B (C-RING1B) of the Polycomb complex; in all those interactions, residues around Ala33 and Thr68 (the ‘hot-spot’ region) of NUPR1 intervene. Its paralogue, NUPR1L, is also expressed in response to DNA damage, it is p53-regulated, and its expression down-regulates that of the NUPR1 gene. In this work, we characterized the conformational preferences of isolated NUPR1L and its possible interactions with the same molecular partners of NUPR1. Our results show that NUPR1L was an oligomeric IDP from pH 2.0 to 12.0, as judged by steady-state fluorescence, circular dichroism (CD), dynamic light scattering, 1D 1H-NMR (nuclear magnetic resonance), and as indicated by structural modelling. However, in contrast with NUPR1, there was evidence of local helical- or turn-like structures; these structures were not rigid, as judged by the lack of sigmoidal behaviour in the chemical and thermal denaturation curves obtained by CD and fluorescence. Interestingly enough, NUPR1L interacted with prothymosin α and C-RING1B, and with a similar affinity to that of NUPR1 (in the low micromolar range). Moreover, NUPR1L hetero-associated with NUPR1 with an affinity of 0.4 µM and interacted with the ‘hot-spot’ region of NUPR1. Thus, we suggest that the regulation of NUPR1 gene by NUPR1L does not only happen at the DNA level, but it could also involve direct interactions with NUPR1 natural partners.

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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