ReviewJournal of molecular biology2011
Probing membrane protein unfolding with pulse proteolysis.
Review in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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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
16 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Fundamentals to function: Quantitative and scalable approaches for measuring protein stability.Cell systems · 2021Review
- Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway.Nature communications · 2019Article
- Kinetic stability of membrane proteins.Biophysical reviews · 2017Review
- Time, space, and disorder in the expanding proteome universe.Proteomics · 2017Article
- The safety dance: biophysics of membrane protein folding and misfolding in a cellular context.Quarterly reviews of biophysics · 2015Article
- Bacteriorhodopsin folds through a poorly organized transition state.Journal of the American Chemical Society · 2014Article
- Measuring membrane protein stability under native conditions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Folding the proteome.Trends in biochemical sciences · 2013Review
- Reversible folding of human peripheral myelin protein 22, a tetraspan membrane protein.Biochemistry · 2013Article
- Simplified proteomics approach to discover protein-ligand interactions.Protein science : a publication of the Protein Society · 2012Article
- Cystathionine beta-synthase mutants exhibit changes in protein unfolding: conformational analysis of misfolded variants in crude cell extracts.Journal of inherited metabolic disease · 2012Article
- Revisiting the folding kinetics of bacteriorhodopsin.Protein science : a publication of the Protein Society · 2012Article
- Knot formation in newly translated proteins is spontaneous and accelerated by chaperonins.Nature chemical biology · 2011Article
- Energetics-based discovery of protein-ligand interactions on a proteomic scale.Journal of molecular biology · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Technical challenges have greatly impeded the investigation of membrane protein folding and unfolding. To develop a new tool that facilitates the study of membrane proteins, we tested pulse proteolysis as a probe for membrane protein unfolding. Pulse proteolysis is a method to monitor protein folding and unfolding, which exploits the significant difference in proteolytic susceptibility between folded and unfolded proteins. This method requires only a small amount of protein and, in many cases, may be used with unpurified proteins in cell lysates. To evaluate the effectiveness of pulse proteolysis as a probe for membrane protein unfolding, we chose Halobacterium halobium bacteriorhodopsin (bR) as a model system. The denaturation of bR in SDS has been investigated extensively by monitoring the change in the absorbance at 560 nm (A(560)). In this work, we demonstrate that denaturation of bR by SDS results in a significant increase in its susceptibility to proteolysis by subtilisin. When pulse proteolysis was applied to bR incubated in varying concentrations of SDS, the remaining intact protein determined by electrophoresis shows a cooperative transition. The midpoint of the cooperative transition (C(m)) shows excellent agreement with that determined by A(560). The C(m) values determined by pulse proteolysis for M56A and Y57A bRs are also consistent with the measurements made by A(560). Our results suggest that pulse proteolysis is a quantitative tool to probe membrane protein unfolding. Combining pulse proteolysis with Western blotting may allow the investigation of membrane protein unfolding in situ without overexpression or purification.
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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.