ArticleThe Journal of biological chemistry2011
Ligand-modulated parallel mechanical unfolding pathways of maltose-binding proteins.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 50 citations in OpenAlex.
- Retracing the evolution of a modern periplasmic binding protein.Protein science : a publication of the Protein Society · 2023Article
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
- Structure dictates the mechanism of ligand recognition in the histidine and maltose binding proteins.Current research in structural biology · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Thermodynamics and folding landscapes of large proteins from a statistical mechanical model.Current research in structural biology · 2019Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.Scientific reports · 2018Article
- Force Spectroscopy of theThe Journal of biological chemistry · 2017Article
- Article
- Significance of 1B and 2B domains in modulating elastic properties of lamin A.Scientific reports · 2016Article
- The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins.Nature communications · 2015Article
- Application of merged spectroscopic data combined with chemometric analysis for resolution of hemoglobin intermediates during chemical unfolding.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2015Article
- Small peptide binding stiffens the ubiquitin-like protein SUMO1.Biophysical journal · 2015Article
- Identifying sequential substrate binding at the single-molecule level by enzyme mechanical stabilization.ACS nano · 2015Article
- Preventing disulfide bond formation weakens non-covalent forces among lysozyme aggregates.PloS one · 2014Article
- Article
- Single-molecule studies on PolySUMO proteins reveal their mechanical flexibility.Biophysical journal · 2013Article
- Analysis of the REJ Module of Polycystin-1 Using Molecular Modeling and Force-Spectroscopy Techniques.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2013Article
- Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.Biophysical journal · 2012Article
- Variation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA.PloS one · 2012Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Protein folding and unfolding are complex phenomena, and it is accepted that multidomain proteins generally follow multiple pathways. Maltose-binding protein (MBP) is a large (a two-domain, 370-amino acid residue) bacterial periplasmic protein involved in maltose uptake. Despite the large size, it has been shown to exhibit an apparent two-state equilibrium unfolding in bulk experiments. Single-molecule studies can uncover rare events that are masked by averaging in bulk studies. Here, we use single-molecule force spectroscopy to study the mechanical unfolding pathways of MBP and its precursor protein (preMBP) in the presence and absence of ligands. Our results show that MBP exhibits kinetic partitioning on mechanical stretching and unfolds via two parallel pathways: one of them involves a mechanically stable intermediate (path I) whereas the other is devoid of it (path II). The apoMBP unfolds via path I in 62% of the mechanical unfolding events, and the remaining 38% follow path II. In the case of maltose-bound MBP, the protein unfolds via the intermediate in 79% of the cases, the remaining 21% via path II. Similarly, on binding to maltotriose, a ligand whose binding strength with the polyprotein is similar to that of maltose, the occurrence of the intermediate is comparable (82% via path I) with that of maltose. The precursor protein preMBP also shows a similar behavior upon mechanical unfolding. The percentages of molecules unfolding via path I are 53% in the apo form and 68% and 72% upon binding to maltose and maltotriose, respectively, for preMBP. These observations demonstrate that ligand binding can modulate the mechanical unfolding pathways of proteins by a kinetic partitioning mechanism. This could be a general mechanism in the unfolding of other large two-domain ligand-binding proteins of the bacterial periplasmic space.
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