ReviewProtein science : a publication of the Protein Society2014
Life at the border: adaptation of proteins to anisotropic membrane environment.
Review in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Dynamic nature of Staphylococcus aureus type I signal peptidases.Biophysical journal · 2025Article
- Asymmetric membrane properties through a protein lens.Faraday discussions · 2025Article
- Amino Acid Substitutions in Bacteriocin Lactolisterin BU Reveal Functional Domains Involved in Biological Activity AgainstMolecules (Basel, Switzerland) · 2025Article
- Kingdom-specific lipid unsaturation calibrates sequence evolution in membrane arm subunits of eukaryotic respiratory complexes.Nature communications · 2025Article
- Sequence-dependent scale for translocon-mediated insertion of interfacial helices in membranes.Science advances · 2025Article
- The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins.Membranes · 2022Article
- GeTFEP: A general transfer free energy profile of transmembrane proteins.Protein science : a publication of the Protein Society · 2020Article
- MemSTATS: A Benchmark Set of Membrane Protein Symmetries and Pseudosymmetries.Journal of molecular biology · 2020Article
- Conformational Dynamics Govern the Free-Energy Landscape of a Membrane-Interacting Protein.ACS omega · 2018Article
- Outer membrane protein folding from an energy landscape perspective.BMC biology · 2017Review
- Characterizing Residue-Bilayer Interactions Using Gramicidin A as a Scaffold and Tryptophan Substitutions as Probes.Journal of chemical theory and computation · 2017Article
- Review
- C≡N stretching vibration of 5-cyanotryptophan as an infrared probe of protein local environment: what determines its frequency?Physical chemistry chemical physics : PCCP · 2016Article
- Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015Review
- Detecting local heterogeneity and ionization ability in the head group region of different lipidic phases using modified fluorescent probes.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
This review discusses main features of transmembrane (TM) proteins which distinguish them from water-soluble proteins and allow their adaptation to the anisotropic membrane environment. We overview the structural limitations on membrane protein architecture, spatial arrangement of proteins in membranes and their intrinsic hydrophobic thickness, co-translational and post-translational folding and insertion into lipid bilayers, topogenesis, high propensity to form oligomers, and large-scale conformational transitions during membrane insertion and transport function. Special attention is paid to the polarity of TM protein surfaces described by profiles of dipolarity/polarizability and hydrogen-bonding capacity parameters that match polarity of the lipid environment. Analysis of distributions of Trp resides on surfaces of TM proteins from different biological membranes indicates that interfacial membrane regions with preferential accumulation of Trp indole rings correspond to the outer part of the lipid acyl chain region-between double bonds and carbonyl groups of lipids. These "midpolar" regions are not always symmetric in proteins from natural membranes. We also examined the hydrophobic effect that drives insertion of proteins into lipid bilayer and different free energy contributions to TM protein stability, including attractive van der Waals forces and hydrogen bonds, side-chain conformational entropy, the hydrophobic mismatch, membrane deformations, and specific protein-lipid binding.
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