ArticleJournal of molecular biology2008
Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Mechanistic Insight into the Mechanical Unfolding of the Integral Membrane Diacylglycerol Kinase.JACS Au · 2024Article
- Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation.International journal of molecular sciences · 2023Article
- An overview of germline variations in genes of primary immunodeficiences through integrative analysis of ClinVar, HGMDHuman genetics · 2021Article
- Free-energy changes of bacteriorhodopsin point mutants measured by single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Homology modeling and global computational mutagenesis of human myosin VIIa.Journal of analytical & pharmaceutical research · 2021Article
- Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway.Nature communications · 2019Article
- Global computational mutagenesis of domain structures associated with inherited eye disease.Scientific reports · 2019Article
- Forced Unfolding Mechanism of Bacteriorhodopsin as Revealed by Coarse-Grained Molecular Dynamics.Biophysical journal · 2016Article
- Distributions of experimental protein structures on coarse-grained free energy landscapes.The Journal of chemical physics · 2015Article
- Observing a lipid-dependent alteration in single lactose permeases.Structure (London, England : 1993) · 2015Article
- Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis.PloS one · 2015Article
- Substrate-induced changes in the structural properties of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.Biochimica et biophysica acta · 2014Review
- Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor.Structure (London, England : 1993) · 2012Article
- Fuzzy oil drop model to interpret the structure of antifreeze proteins and their mutants.Journal of molecular modeling · 2012Article
- Locating an extracellular K+-dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Using single-molecule force spectroscopy, we investigated the effect of single point mutations on the energy landscape and unfolding pathways of the transmembrane protein bacteriorhodopsin. We show that the unfolding energy barriers in the energy landscape of the membrane protein followed a simple two-state behavior and represent a manifestation of many converging unfolding pathways. Although the unfolding pathways of wild-type and mutant bacteriorhodopsin did not change, indicating the presence of same ensemble of structural unfolding intermediates, the free energies of the rate-limiting transition states of the bacteriorhodopsin mutants decreased as the distance of those transition states to the folded intermediate states decreased. Thus, all mutants exhibited Hammond behavior and a change in the free energies of the intermediates along the unfolding reaction coordinate and, consequently, their relative occupancies. This is the first experimental proof showing that point mutations can reshape the free energy landscape of a membrane protein and force single proteins to populate certain unfolding pathways over others.
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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.