ArticleBiophysical journal2011
Single molecule force spectroscopy reveals that electrostatic interactions affect the mechanical stability of proteins.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Article
- Single-Molecule Force Spectroscopy Reveals Stability of mitoNEET and its [2Fe2Se] Cluster in Weakly Acidic and Basic Solutions.ChemistryOpen · 2022Article
- Detection of weak non-covalent cation-π interactions in NGAL by single-molecule force spectroscopy.Nano research · 2022Article
- The dual role of SrbA from Paracoccidioides lutzii: a hypoxic regulator.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021Article
- The molecular mechanisms underlying mussel adhesion.Nanoscale advances · 2019Review
- Force-induced chemical reactions on the metal centre in a single metalloprotein molecule.Nature communications · 2015Article
- Effect of electrostatics on aggregation of prion protein Sup35 peptide.Journal of physics. Condensed matter : an Institute of Physics journal · 2012Article
- Worm-like Ising model for protein mechanical unfolding under the effect of osmolytes.Biophysical journal · 2012Article
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5 authors.
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Abstract
It is well known that electrostatic interactions play important roles in determining the thermodynamic stability of proteins. However, the investigation into the role of electrostatic interactions in mechanical unfolding of proteins has just begun. Here we used single molecule atomic force microscopy techniques to directly evaluate the effect of electrostatic interactions on the mechanical stability of a small protein GB1. We engineered a bi-histidine motif into the force-bearing region of GB1. By varying the pH, histidine residues can switch between protonated and deprotonated states, leading to the change of the electrostatic interactions between the two histidine residues. We found that the mechanical unfolding force of the engineered protein decreased by ∼34% (from 115 pN to 76 pN) on changing the pH from 8.5 to 3, due to the increased electrostatic repulsion between the two positively charged histidines at acidic pH. Our results demonstrated that electrostatic interactions can significantly affect the mechanical stability of elastomeric proteins, and modulating the electrostatic interactions of key charged residues can become a promising method for regulating the mechanical stability of elastomeric proteins.
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