ReviewBiomolecules2014
Kinetics and thermodynamics of membrane protein folding.
Review in Biomolecules, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Fluorescence phasor analysis: basic principles and biophysical applications.Biophysical reviews · 2025Review
- Probing the Dynamics of Yersinia Adhesin A (YadA) in Outer Membranes Hints at Requirements for β-Barrel Membrane Insertion.Journal of the American Chemical Society · 2025Article
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Single-Step Protocol for Isolating the Recombinant Extracellular Domain of the Luteinizing Hormone Receptor from theCurrent issues in molecular biology · 2022Article
- Connexins and Pannexins-Similarities and Differences According to the FOD-M Model.Biomedicines · 2022Article
- Thermal inactivation scaling applied for SARS-CoV-2.Biophysical journal · 2021Article
- Differential compartmental processing and phosphorylation of pathogenic human tau and native mouse tau in the line 66 model of frontotemporal dementia.The Journal of biological chemistry · 2020Article
- A versatile tool in controlling aggregation and Ag nanoparticles assisted in vitro folding of thermally denatured zDHFR.Biochemistry and biophysics reports · 2020Article
- Enhanced oligomerization of full-length RAGE by synergy of the interaction of its domains.Scientific reports · 2019Article
- Thermal proteome profiling in bacteria: probing protein stateMolecular systems biology · 2018Article
- Kinetic stability of membrane proteins.Biophysical reviews · 2017Review
- 2-Methyl-2,4-pentanediol (MPD) boosts as detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene polymerization.Beilstein journal of organic chemistry · 2017Article
- Reversible Unfolding of Rhomboid Intramembrane Proteases.Biophysical journal · 2016Article
- Modulation of plasma membrane Ca2+-ATPase by neutral phospholipids: effect of the micelle-vesicle transition and the bilayer thickness.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Understanding protein folding has been one of the great challenges in biochemistry and molecular biophysics. Over the past 50 years, many thermodynamic and kinetic studies have been performed addressing the stability of globular proteins. In comparison, advances in the membrane protein folding field lag far behind. Although membrane proteins constitute about a third of the proteins encoded in known genomes, stability studies on membrane proteins have been impaired due to experimental limitations. Furthermore, no systematic experimental strategies are available for folding these biomolecules in vitro. Common denaturing agents such as chaotropes usually do not work on helical membrane proteins, and ionic detergents have been successful denaturants only in few cases. Refolding a membrane protein seems to be a craftsman work, which is relatively straightforward for transmembrane β-barrel proteins but challenging for α-helical membrane proteins. Additional complexities emerge in multidomain membrane proteins, data interpretation being one of the most critical. In this review, we will describe some recent efforts in understanding the folding mechanism of membrane proteins that have been reversibly refolded allowing both thermodynamic and kinetic analysis. This information will be discussed in the context of current paradigms in the protein folding field.
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