ArticleBiophysical journal2011
Inhibitor binding increases the mechanical stability of staphylococcal nuclease.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Inhibitory mechanism of peptides with a repeating hydrophobic and hydrophilic residue pattern on interleukin-10.Human vaccines & immunotherapeutics · 2017Article
- Capsid-Targeted Viral Inactivation: A Novel Tactic for Inhibiting Replication in Viral Infections.Viruses · 2016Review
- Modular, Nondegenerate Polyprotein Scaffolds for Atomic Force Spectroscopy.Biomacromolecules · 2016Article
- Monoterpenes as nitrofurantoin resistance modulating agents: minimal structural requirements, molecular dynamics simulations, and the effect of piperitone on the emergence of nitrofurantoin resistance in Enterobacteriaceae.Journal of molecular modeling · 2015Article
- Identifying sequential substrate binding at the single-molecule level by enzyme mechanical stabilization.ACS nano · 2015Article
- Improving single molecule force spectroscopy through automated real-time data collection and quantification of experimental conditions.Ultramicroscopy · 2014Article
- Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin.PLoS computational biology · 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
- A nanoscale force probe for gauging intermolecular interactions.Angewandte Chemie (International ed. in English) · 2012Article
- Variation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA.PloS one · 2012Article
- Nanomechanics of streptavidin hubs for molecular materials.Advanced materials (Deerfield Beach, Fla.) · 2011Article
- Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Biophysical journal · 2011Article
- Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.The Journal of biological chemistry · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Staphylococcal nuclease (SNase) catalyzes the hydrolysis of DNA and RNA in a calcium-dependent fashion. We used AFM-based single-molecule force spectroscopy to investigate the mechanical stability of SNase alone and in its complex with an SNase inhibitor, deoxythymidine 3',5'-bisphosphate. We found that the enzyme unfolds in an all-or-none fashion at ∼26 pN. Upon binding to the inhibitor, the mechanical unfolding forces of the enzyme-inhibitor complex increase to ∼50 pN. This inhibitor-induced increase in the mechanical stability of the enzyme is consistent with the increased thermodynamical stability of the complex over that of SNase. Because of its strong mechanical response to inhibitor binding, SNase, a model protein folding system, offers a unique opportunity for studying the relationship between enzyme mechanics and catalysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.