ArticleBiophysical journal2007
The effect of protein complexation on the mechanical stability of Im9.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
- Small peptide binding stiffens the ubiquitin-like protein SUMO1.Biophysical journal · 2015Article
- Recent applications of boxed molecular dynamics: a simple multiscale technique for atomistic simulations.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2014Article
- Article
- Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin.PLoS computational biology · 2013Article
- Ligand-modulated parallel mechanical unfolding pathways of maltose-binding proteins.The Journal of biological chemistry · 2011Article
- Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.The Journal of biological chemistry · 2011Article
- Inhibitor binding increases the mechanical stability of staphylococcal nuclease.Biophysical journal · 2011Article
- Identification of a mechanical rheostat in the hydrophobic core of protein L.Journal of molecular biology · 2009Article
- Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation.The Journal of biological chemistry · 2009Article
- A functional single-molecule binding assay via force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Force mode microscopy can be used to examine the effect of mechanical manipulation on the noncovalent interactions that stabilize proteins and their complexes. Here we describe the effect of complexation by the high affinity protein ligand E9 on the mechanical resistance of the simple four-helical protein, Im9. When concatenated into a construct of alternating I27 domains, Im9 unfolded below the thermal noise limit of the instrument ( approximately 20 pN). Complexation of E9 had little effect on the mechanical resistance of Im9 (unfolding force approximately 30 pN) despite the high avidity of this complex (K(d) approximately 10 fM).
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Registered trials
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