Influence of macromolecular crowding on the charge regulation of intrinsically disordered proteins

Soft Matter ◽  
2021 ◽  
Author(s):  
Pablo M. Blanco ◽  
Sergio Madurga ◽  
Josep L. Garcés ◽  
Francesc Mas ◽  
Rita S. Dias
Keyword(s):  
Monte Carlo ◽  
Intrinsically Disordered Proteins ◽  
Disordered Proteins ◽  
Grand Canonical Monte Carlo ◽  
Histatin 5 ◽  
Charge Regulation ◽  
Intrinsically Disordered ◽  
Conformational Properties ◽  
Β Amyloid ◽  
Grand Canonical

The coupling between the ionization and conformational properties of two IDPs, histatin-5 and β-amyloid 42, in the presence of neutral and charged crowders is studied by performing semi-grand canonical Monte Carlo simulations.

scholarly journals Quantitative Determination of the Conformational Properties of Partially Folded and Intrinsically Disordered Proteins Using NMR Dipolar Couplings

Structure ◽  
2009 ◽  
Vol 17 (9) ◽  
pp. 1169-1185 ◽  
Author(s):  
Malene Ringkjøbing Jensen ◽  
Phineus R.L. Markwick ◽  
Sebastian Meier ◽  
Christian Griesinger ◽  
Markus Zweckstetter ◽  
...  
Keyword(s):  
Quantitative Determination ◽  
Intrinsically Disordered Proteins ◽  
Dipolar Couplings ◽  
Disordered Proteins ◽  
Intrinsically Disordered ◽  
Conformational Properties

scholarly journals Dynamical Oligomerisation of Histidine Rich Intrinsically Disordered Proteins Is Regulated through Zinc-Histidine Interactions

Biomolecules ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 168 ◽  
Author(s):  
Carolina Cragnell ◽  
Lasse Staby ◽  
Samuel Lenton ◽  
Birthe Kragelund ◽  
Marie Skepö
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Intrinsically Disordered Proteins ◽  
Divalent Cations ◽  
Disordered Proteins ◽  
Resonance Spectroscopy ◽  
Binding Motifs ◽  
Histatin 5 ◽  
X Ray ◽  
Intrinsically Disordered ◽  
X Ray Scattering

Intrinsically disordered proteins (IDPs) can form functional oligomers and in some cases, insoluble disease related aggregates. It is therefore vital to understand processes and mechanisms that control pathway distribution. Divalent cations including Zn2+ can initiate IDP oligomerisation through the interaction with histidine residues but the mechanisms of doing so are far from understood. Here we apply a multi-disciplinary approach using small angle X-ray scattering, nuclear magnetic resonance spectroscopy, calorimetry and computations to show that that saliva protein Histatin 5 forms highly dynamic oligomers in the presence of Zn2+. The process is critically dependent upon interaction between Zn2+ ions and distinct histidine rich binding motifs which allows for thermodynamic switching between states. We propose a molecular mechanism of oligomerisation, which may be generally applicable to other histidine rich IDPs. Finally, as Histatin 5 is an important saliva component, we suggest that Zn2+ induced oligomerisation may be crucial for maintaining saliva homeostasis.

Conformational properties of intrinsically disordered proteins bound to the surface of silica nanoparticles

2018 ◽  
Vol 1862 (7) ◽  
pp. 1556-1564 ◽  
Author(s):  
Michele Vitali ◽  
Valentina Rigamonti ◽  
Antonino Natalello ◽  
Barbara Colzani ◽  
Svetlana Avvakumova ◽  
...  
Keyword(s):  
Silica Nanoparticles ◽  
Intrinsically Disordered Proteins ◽  
Disordered Proteins ◽  
Intrinsically Disordered ◽  
Conformational Properties

scholarly journals Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1095
Author(s):  
Joel Markgren ◽  
Mikael Hedenqvist ◽  
Faiza Rasheed ◽  
Marie Skepö ◽  
Eva Johansson
Keyword(s):  
Monte Carlo ◽  
Monte Carlo Simulations ◽  
Disulfide Bonds ◽  
Intrinsically Disordered Proteins ◽  
Coarse Grained ◽  
Disordered Proteins ◽  
Cysteine Residues ◽  
Chain Flexibility ◽  
Intrinsically Disordered ◽  
Intermolecular Disulfide Bonds

Gluten protein crosslinking is a predetermined process where specific intra- and intermolecular disulfide bonds differ depending on the protein and cysteine motif. In this article, all-atom Monte Carlo simulations were used to understand the formation of disulfide bonds in gliadins and low molecular weight glutenin subunits (LMW-GS). The two intrinsically disordered proteins appeared to contain mostly turns and loops and showed “self-avoiding walk” behavior in water. Cysteine residues involved in intramolecular disulfide bonds were located next to hydrophobic peptide sections in the primary sequence. Hydrophobicity of neighboring peptide sections, synthesis chronology, and amino acid chain flexibility were identified as important factors in securing the specificity of intramolecular disulfide bonds formed directly after synthesis. The two LMW-GS cysteine residues that form intermolecular disulfide bonds were positioned next to peptide sections of lower hydrophobicity, and these cysteine residues are more exposed to the cytosolic conditions, which influence the crosslinking behavior. In addition, coarse-grained Monte Carlo simulations revealed that the protein folding is independent of ionic strength. The potential molecular behavior associated with disulfide bonds, as reported here, increases the biological understanding of seed storage protein function and provides opportunities to tailor their functional properties for different applications.

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