ArticleJournal of the American Chemical Society2009
Protein unfolding with a steric trap.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Scalable production of monovalent streptavidin with high yield and purity.Scientific reports · 2026Article
- Label-Free SERS Fingerprinting of Neuroprotein Conformational Dynamics in Human Saliva.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Untangling the complexity of membrane protein folding.Current opinion in structural biology · 2022Review
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- The rhomboid protease GlpG has weak interaction energies in its active site hydrogen bond network.The Journal of general physiology · 2019Article
- Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Journal of molecular biology · 2018Review
- Steric trapping reveals a cooperativity network in the intramembrane protease GlpG.Nature chemical biology · 2016Article
- Design and characterization of a membrane protein unfolding platform in lipid bilayers.PloS one · 2015Article
- Plug-and-play pairing via defined divalent streptavidins.Journal of molecular biology · 2014Article
- Measuring membrane protein stability under native conditions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Membrane proteins can have high kinetic stability.Journal of the American Chemical Society · 2013Article
- Measuring transmembrane helix interaction strengths in lipid bilayers using steric trapping.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Protein unfolding and degradation by the AAA+ Lon protease.Protein science : a publication of the Protein Society · 2012Article
- Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments.Journal of the American Chemical Society · 2011Article
- Molecular simulations of mutually exclusive folding in a two-domain protein switch.Biophysical journal · 2011Article
- Method to measure strong protein-protein interactions in lipid bilayers using a steric trap.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The study of protein folding requires a method to drive unfolding, which is typically accomplished by altering solution conditions to favor the denatured state. This has the undesirable consequence that the molecular forces responsible for configuring the polypeptide chain are also changed. It would therefore be useful to develop methods that can drive unfolding without the need for destabilizing solvent conditions. Here we introduce a new method to accomplish this goal, which we call steric trapping. In the steric trap method, the target protein is labeled with two biotin tags placed close in space so that both biotin tags can only be bound by streptavidin when the protein unfolds. Thus, binding of the second streptavidin is energetically coupled to unfolding of the target protein. Testing the method on a model protein, dihydrofolate reductase (DHFR), we find that streptavidin binding can drive unfolding and that the apparent binding affinity reports on changes in DHFR stability. Finally, by employing the slow off-rate of wild-type streptavidin, we find that DHFR can be locked in the unfolded state. The steric trap method provides a simple method for studying aspects of protein folding and stability in native solvent conditions, could be used to specifically unfold selected domains, and could be applicable to membrane proteins.
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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.