The DOI matches its Crossref record; 224 of the 224 references it cites were found in a registry or an index.
Lipid–protein interactions in biological membranes: a structural perspective
Open accessAbstract
Lipid molecules bound to membrane proteins are resolved in some high-resolution structures of membrane proteins. An analysis of these structures provides a framework within which to analyse the nature of lipid-protein interactions within membranes. Membrane proteins are surrounded by a shell or annulus of lipid molecules, equivalent to the solvent layer surrounding a water-soluble protein. The lipid bilayer extends right up to the membrane protein, with a uniform thickness around the protein. The surface of a membrane protein contains many shallow grooves and protrusions to which the fatty acyl chains of the surrounding lipids conform to provide tight packing into the membrane. An individual lipid molecule will remain in the annular shell around a protein for only a short period of time. Binding to the annular shell shows relatively little structural specificity. As well as the annular lipid, there is evidence for other lipid molecules bound between the transmembrane alpha-helices of the protein; these lipids are referred to as non-annular lipids. The average thickness of the hydrophobic domain of a membrane protein is about 29 A, with a few proteins having significantly smaller or greater thicknesses than the average. Hydrophobic mismatch between a membrane protein and the surrounding lipid bilayer generally leads to only small changes in membrane thickness. Possible adaptations in the protein to minimise mismatch include tilting of the helices and rotation of side chains at the ends of the helices. Packing of transmembrane alpha-helices is dependent on the chain length of the surrounding phospholipids. The function of membrane proteins is dependent on the thickness of the surrounding lipid bilayer, sometimes on the presence of specific, usually anionic, phospholipids, and sometimes on the phase of the phospholipid.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Fatty acyl chain length alters binding constants of several membrane proteins [169], making it tempting to speculate that VLCFAs might alter neural cell membrane structure, stability, and function [170].”
From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [169]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
Doyle, D., Morais-Cabral, J. H., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., & MacKinnon, R. (1998) · Science · doi:10.1126/science.280.5360.69 · Cited by 6,851
Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria
McDermott, G., Prince, S. M., Freer, A. A., Hawthornthwaite, A. M., Papiz, M. Z., Cogdell, R. J., & Isaacs, N. W. (1995) · Nature · doi:10.1038/374517a0 · Cited by 2,741
Nagle, J. F., & Tristram‐Nagle, S. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(00)00016-2 · Cited by 2,660
Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
Jordan, P., Fromme, P., Witt, H. T., Klukas, O., Saenger, W., & Krauß, N. (2001) · Nature · doi:10.1038/35082000 · Cited by 2,494
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,102
Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution
Zhou, Y., Morais-Cabral, J. H., Kaufman, A., & MacKinnon, R. (2001) · Nature · doi:10.1038/35102009 · Cited by 2,092
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,019
Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
Toyoshima, C., Nakasako, M., NOMURA, H., & Ogawa, H. (2000) · Nature · doi:10.1038/35015017 · Cited by 1,811
Structural determinants of water permeation through aquaporin-1
Murata, K., Mitsuoka, K., Hirai, T., Walz, T., Agre, P. C., Heymann, J. B., Engel, A. H., & Fujiyoshi, Y. (2000) · Nature · doi:10.1038/35036519 · Cited by 1,810
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
White, S. H., & Wimley, W. C. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.319 · Cited by 1,767
Research works printed but not linked: 6
- Davoust, 1982, J. Magn. Res., 48, 475
- Mouritsen, 1993, Annu. Rev. Biophys. Bioeng., 22, 145, 10.1146/annurev.bb.22.060193.001045 · DOI
- Verma, 1983, Adv. Lipid Res., 20, 257
- White, 1999, Annu. Rev. Biophys. Biomol. Struct., 28, 319, 10.1146/annurev.biophys.28.1.319 · DOI
- Hoffmann, 1980, J. Mol. Biol., 141, 132
- Litman, 1996, vol. 2A, 1
Cited by
Sorted by citations
Items 801–885 of 885
An, E. S., Choi, J. S., & Lee, D. K. (2014) · Journal of the Society of Cosmetic Scientists of Korea · doi:10.15230/scsk.2014.40.2.163
Membrane Protein Simulations: Modelling a Complex Environment
Bond, P. J., Cuthbertson, J. M., Deol, S. S., et al. (2006) · Springer eBooks · doi:10.1007/3-540-31618-3_1
“On the basis of analysis of membrane protein structures [50] and from biophysical experiments on membrane protein models it has been shown that two classes of amino acids play an important role in locking a membrane protein into a lipid bilayer [26].”
BackgroundMolecular Dynamics Simulations of Lipid Bilayers with Incorporated Peptides
Melicherčík, M., Hianik, T., & Urban, J. (2014) · Challenges and advances in computational chemistry and physics · doi:10.1007/978-94-017-9257-8_8
“Killian [39] or Lee [40]).”
Fluoroquinolone Transport Through Bacterial Membranes: A Multi-Technique Approach
Sousa, C. F. (2014) · Open Repository of the University of Porto (University of Porto) · doi:10.34626/5pjk-5x66
Trojanowski, N. (2015) · Brock University Digital Repository (Brock University)
Ion traffic across cellular membranes
Gallaher, J. A. (2010) · The Scholarship East Carolina University's Institutional Repository (East Carolina University)
Mecanismo de acción de la toxina alfa hemolisina de Escherichia coli
Exactas, C. (2015)
Lipid Exchange by Ultracentrifugation
Drachmann, N. D., & Olesen, C. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3179-8_35
Ward, M. E. (2016) · The Atrium (University of Guelph)
Mechanobiology of the Cell Membrane
Butler, P. J., Muddana, H. S., & Farag, S. (2014) · CRC Press eBooks · doi:10.1201/b17612-6
Tarek, M. (2010) · Water · doi:10.1201/b11671-13
Membrane Protein Biogenesis and Assembly at the Endoplasmic Reticulum Membrane
Bhanu, M. K., & Kendall, D. A. (2011) · CRC Press eBooks · doi:10.1201/b11018-11
Microfluidic Devices for Membrane Protein Nanoparticle Formation
Wu, H.-J. (2013) · CU Scholar (University of Colorado Boulder)
Use of Fluorescence Resonance Energy Transfer for Detection of Lattice Formation in ASR
Baek, J. (2015) · The Atrium (University of Guelph)
Mass Spectrometry-Based Structural Analysis of Photosynthetic Protein Assemblies
Lu, Y. (2017) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7th8k4q
“122 6.3.3 Native MS and IM-MS Analysis of NTD, CTD and FRP complex ................................. 122 6.3.4 Activity assays .................................................................................................................. 122 6.3.5 Cross-linking and LC-MS ...........................................…”
BackgroundInfluentialStudying Protein Organization in Cellular Membranes by High-Resolution Microscopy
Saka, S. K. (2014) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4715
Membrane Proteins and Their Natural Environment
Popot, J. (2018) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-73148-3_1
Characterization of platelet disorders using quantitative proteomics
Solari (2018) · Research Publications (Maastricht University) · doi:10.26481/dis.20180626fs
Rower, D. A., & Atzberger, P. J. (2019) · arXiv (Cornell University)
Luckey, M. (2008) · Cambridge University Press eBooks · doi:10.1017/cbo9780511811098.009
Investigating Bacterial Lipopolysaccharides and Interactions with Antimicrobial Peptides
Strauss, J. D. (2009) · Digital WPI
Schwann cell differentiation in Charcot-Marie-Tooth disease 1 A (CMT1A)
Abdelaal, T. A. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7331
Quad Lipid Bilayer Module with 1-GΩ Series Resistors Toward Quantitative Stochastic-Biosensors
Ito, Y., Osaki, T., Kamiya, K., et al. (2019) · doi:10.1109/transducers.2019.8808191
“of information in and out of cells, and greatly influences physiological functions such as drug response and immune response [1].”
BackgroundBubble-Assisted in-Situ Re-Formation of Artificial Bilayer
Hashimoto, I., Sugiura, H., Osaki, T., et al. (2020) · Proceedings, IEEE micro electro mechanical systems · doi:10.1109/mems46641.2020.9056202
Investigations into Allosteric Mechanisms of G Protein Activation
Thaker, T. M. (2013)
Wilson, J. (2020) · Scholars' Bank (University of Oregon)
Non-lysosomal accumulation of glucosylceramide alters cytoskeletal dynamics causing globozoospermia
Raju, D. N. (2015) · bonndoc (University of Bonn)
Hameed, R. M. A. (2013) · bonndoc (University of Bonn)
Remers, N. (2013) · Utrecht University Repository (Utrecht University)
Förster Resonance Energy Transfer as a Tool for Quantification of Protein–Lipid Selectivity
Loura, L. M. S., PRIETO, M. J. E., & Fernandes, F. (2012) · Methods in molecular biology · doi:10.1007/978-1-0716-5054-7_16
Inada, M., Iwamoto, M., Yoshida, N., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.08.479071
Silvius, J. R. (2013) · Colloquium Series on Building Blocks of the Cell Cell Structure and Function · doi:10.4199/c00076ed1v01y201303bbc001
González, R., Figueiredo, P., & Carvalho, A. T. P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.09.479755
“However, five of the new sequences (seq2, seq3, seq7, seq9, and seq10) have hydrophobic faces, which are said to be features of biologically active peptides, as these hydrophobic residues may insert between the membranes’ lipid acyl chains, allowing for binding and crossing the membrane [31].”
Background(2017) · Wiley-VCH eBooks · doi:10.1002/9783527698448.ch10
KAMIYA, K., Osaki, T., & Takeuchi, S. (2015) · Electrochemistry · doi:10.5796/electrochemistry.83.1096
Wang, Z. (2014) · Springer eBooks · doi:10.1007/978-3-642-40872-4_2159-1
Reuning, U., Lössner, D., Wiltschi, B., et al. (2013) · Pan Stanford Publishing eBooks · doi:10.1201/b14900-26
The discovery of antibiotics from soil and the characterization of darobactin analogs
Green, R. (2022) · Digital Repository Service (Northeastern University) · doi:10.17760/d20439214
The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase
Jakob, R. P., Kaur, H., Marzinek, J. K., Green, R., Imai, Y., Bolla, J. R., Agustoni, E., Robinson, C. V., Bond, P. J., Lewis, K., et al. (2022) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s205327332209619x
Dynamic framework for large-scale modeling of membranes and peripheral proteins
Sadeghi, M., & Rosenberger, D. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.03.018
Advanced Techniques for Analyzing the Protein–Lipid Interactions
Anitha, S., Jayasree, R., Kulanthaivel, L., Subbaraj, G. K., & Muthuvel, R. (2024) · Springer eBooks · doi:10.1007/978-981-97-5437-3_10
Färber, N., Mauritz, S. C. F., Huber, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.29.635609
“While no distinct transition could be seen in c) using Laurdan there is an even more pronounced transition after denaturation as compared to the plasma membrane. simulations that the order state of lipids is affected by the conformation of proximal proteins [45].”
Vladkova, R. S. (2025) · Membranes · doi:10.3390/membranes15050143
“As also seen from the lipids of the cyt b 6 f monomer structure (Figure 3, Supplementary Video S2 Material (SupplVideo2)), these 19 annular lipids [136,137] form an ellipse-shaped bilayer shell around the monomer.”
Lapshin, N. K., Piotrovskii, M. S., & Trofimova, M. S. (2025) · Russian Journal of Plant Physiology · doi:10.1134/s102144372560182x
“…by altering physicochemical parameters of the bilayer, such as fluidity or membrane thickness (so-called general interactions), and directly, through specific sterol-binding sites and/or by forming a special lipid “shell” at the protein/bilayer interface (specific interactions) [11, 38–40].”
Youn, T., Ehsan, M., Hariharan, P., Li, X., Moon, Y., Ahmed, W., Byrne, B., Liu, X., Guan, L., & Chae, P. S. (2025) · Journal of Materials Chemistry B · doi:10.1039/d5tb01342a
Death, taxes, and rhomboids: Understanding the ubiquitous roles of the rhomboid protein superfamily
Sawczyc, H., Kosteletos, S., & Lange, A. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110699
“Interestingly, 1,2-dilauroyl-sn -glycero-3-phosphocholine bi-layers are approximately 31 to 33 Å thick, higher than the hydrophobic thickness of GlpG ( � 25 Å by crystal structure determination (71)) and than the average membrane protein thickness of 29 Å (103).”
Стефанович, О. С., & Martsinkevich, A. F. (2014) · Health and Ecology Issues · doi:10.51523/2708-6011.2014-11-1-23
Active regulation of the epidermal growth factor receptor by the membrane bilayerPreprint
Srinivasan, S., Lin, X., Chen, X., Regmi, R., Zhang, B., & Schlau‐Cohen, G. S. (2025) · eLife · doi:10.7554/elife.108789.1
Li, J., Thomson, S., & Monje‐Galvan, V. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01664
Synthesis and protein curing abilities of membrane glycolipids
Wikström, M. (2006) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Spectroscopic function-structure analysis of the SERCA-PLB complex
Dong, X. (2014) · University of Minnesota Digital Conservancy (University of Minnesota)
Pucciarelli, V., Caivano, I., Scieuzo, C., & Falabella, P. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29896-7.00005-6
Active regulation of the epidermal growth factor receptor by the membrane bilayerPreprint
Srinivasan, S., Lin, X., Chen, X., Regmi, R., Zhang, B., & Schlau‐Cohen, G. S. (2026) · eLife · doi:10.7554/elife.108789.2
Lipid Metabolism and Trafficking in the Golgi Apparatus
Parolek, J., Kim, Y., & Burd, C. G. (2026) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-032-16833-7_8
Cardiolipin disperses aquaporin Z tetramers to enhance water permeability
Surya, W., Bharambe, N. G., Tan, P., Basak, S., & Torres, J. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.151540
Variation d'hydrophobicité et structure secondaire des protéines transmembranaires
Paulet, D. (2010) · theses.fr (ABES) · doi:10.70675/e251b6bcz9405z4757zacb0z77fe1f1161f7
Interplay between ABC membrane transporter BmrA and its membrane environment
Paik, S.-J. (2018) · theses.fr (ABES) · doi:10.70675/abd33f46z7071z4244z80a3zdbf6ba1fc28b
Cellular membranes as Quantum-to-Classical Transducers via 1836:1 mass-anisotropyPreprint
Ariyannur, P. S. (2026) · Research Square · doi:10.21203/rs.3.rs-9269552/v1
Plasma membrane invaginations and their diverse cellular functions
Zhu, H. J., Lyons, C. A., Sydor, A., Hilgemann, D., & Brumell, J. (2026) · BMC Biology · doi:10.1186/s12915-026-02615-6
“Interestingly, plancto-mycetes express proteins structurally related to eukaryotic clathrin and coat proteins [324].”
Mu, J., Sedough-Abbasian, D., Mao, L., & Carmali, S. (2026) · ACS Nanoscience Au · doi:10.1021/acsnanoscienceau.6c00033 · Cited by 1
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.05
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.references
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.07
Third Section: Design of a dimeric-nanobody specific for Aβ42 oligomers: the Dimeric-DesAb-O
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.06
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.03
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.04
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.02
Conclusion and Future Perspectives
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.08
Membrane Models and the Pursuit of Coherence
Kervin, T. A., Zhang, Z., Clark, M., Overduin, M., & Zhang, P. (2026) · Biochemistry · doi:10.1021/acs.biochem.6c00367
“132,133 Similarly, it was proposed that cholesterol − phospholipid complexes discussed above could assemble around proteins into long-lived shells.”
Bilayer Elastic Properties Modulate Interface Energetics of Transmembrane β-Barrels
Gupta, S., & Mahalakshmi, R. (2026) · Biochemistry · doi:10.1021/acs.biochem.6c00283
Lioupi, A., Gavriilidou, A. F. M., & Politis, A. (2026) · Chemical Science · doi:10.1039/d6sc04457c · Cited by 1
Rugji, J., Goodman, R. J., Armstrong, M. T., et al. (2026) · Journal of Dairy Science · doi:10.3168/jds.2026-29265
Zhang, W., Shen, J., Zhao, Y., et al. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.151096
Enoki, T. A. (2026) · Biophysical Reviews · doi:10.1007/s12551-026-01468-1
Wang, Z. (2016) · Springer eBooks · doi:10.1007/978-3-662-44324-8_2159
Björnerås, J. (2014) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Regulation of Plant Transporters by Lipids and Microdomains
Simon-Plas, F., Mongrand, S., & Wipf, D. (2010) · Signaling and communication in plants · doi:10.1007/978-3-642-14369-4_13
“Most of the lipid molecules resolved in high-resolution crystal structures of membrane proteins are likely to be nonannular lipids, their strong binding to the protein leading to immobilization of at least part of the lipid molecule so that they appear in the high-resolution structure (Lee 2003).”
Background
Metadata
- Authors
- Lee, A. G.
- Affiliations
- University of Southampton (GB)
- Corresponding author
- Lee, A.G
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 1612
- Issue
- 1
- Pages
- 1-40
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2128882835
- Cited by
- 886
- References
- 224
- Citations by year
- 2026: 31 · 2025: 30 · 2024: 25 · 2023: 16 · 2022: 32 · 2021: 33 · 2020: 31 · 2019: 51 · 2018: 37 · 2017: 33 · 2016: 32 · 2015: 51 · 2014: 47 · 2013: 38 · 2012: 32
- FWCI
- 3.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- protein-lipid interactions, membrane proteins, lipid bilayers, transmembrane helices, hydrophobic mismatch, membrane thickness, helix tilt, anionic phospholipids, lipid phase, membrane protein structure
- MeSH terms
- Animals, Bacteriorhodopsins, Crystallization, Humans, Lipid Bilayers, Membrane Lipids, Membrane Proteins, Protein Structure, Secondary, Photosynthetic Reaction Center Complex Proteins, Hydrophobic and Hydrophilic Interactions
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
