ArticleBiophysical journal2010
Mechanical unfolding of acylphosphatase studied by single-molecule force spectroscopy and MD simulations.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Protein folding mechanism revealed by single-molecule force spectroscopy experiments.Biophysics reports · 2021Article
- Role of Resultant Dipole Moment in Mechanical Dissociation of Biological Complexes.Molecules (Basel, Switzerland) · 2018Article
- Article
- Small peptide binding stiffens the ubiquitin-like protein SUMO1.Biophysical journal · 2015Article
- Sequence analysis on the information of folding initiation segments in ferredoxin-like fold proteins.BMC structural biology · 2014Article
- Article
- Stabilization of a protein conferred by an increase in folded state entropy.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Variation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA.PloS one · 2012Article
- Ligand-modulated parallel mechanical unfolding pathways of maltose-binding proteins.The Journal of biological chemistry · 2011Article
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Authors and funding
9 authors.
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Abstract
Single-molecule manipulation methods provide a powerful means to study protein transitions. Here we combined single-molecule force spectroscopy and steered molecular-dynamics simulations to study the mechanical properties and unfolding behavior of the small enzyme acylphosphatase (AcP). We find that mechanical unfolding of AcP occurs at relatively low forces in an all-or-none fashion and is decelerated in the presence of a ligand, as observed in solution measurements. The prominent energy barrier for the transition is separated from the native state by a distance that is unusually long for alpha/beta proteins. Unfolding is initiated at the C-terminal strand (beta(T)) that lies at one edge of the beta-sheet of AcP, followed by unraveling of the strand located at the other. The central strand of the sheet and the two helices in the protein unfold last. Ligand binding counteracts unfolding by stabilizing contacts between an arginine residue (Arg-23) and the catalytic loop, as well as with beta(T) of AcP, which renders the force-bearing units of the protein resistant to force. This stabilizing effect may also account for the decelerated unfolding of ligand-bound AcP in the absence of force.
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