ArticleBiophysical journal2010
Crystallizing transmembrane peptides in lipidic mesophases.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Solid-state NMR of membrane peptides and proteins in the lipid cubic phase.Biophysical journal · 2025Article
- Intrinsic Lipid Curvature and Bilayer Elasticity as Regulators of Channel Function: A Comparative Single-Molecule Study.International journal of molecular sciences · 2024Article
- Methods of Measuring Mitochondrial Potassium Channels: A Critical Assessment.International journal of molecular sciences · 2022Review
- Probing the structure of nanodiscs using surface-induced dissociation mass spectrometry.Chemical communications (Cambridge, England) · 2020Article
- Functional stability of water wire-carbonyl interactions in an ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Native Mass Spectrometry of Antimicrobial Peptides in Lipid Nanodiscs Elucidates Complex Assembly.Analytical chemistry · 2019Article
- Effect of Site-Specific Intermolecular Lysine-Tryptophan Interactions on the Aggregation of Gramicidin-Based Peptides Leading to Pore Formation in Lipid Membranes.The Journal of membrane biology · 2018Article
- Exploring the in meso crystallization mechanism by characterizing the lipid mesophase microenvironment during the growth of single transmembrane α-helical peptide crystals.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Article
- Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly.Cell reports · 2015Article
- Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes.Acta crystallographica. Section F, Structural biology communications · 2015Review
- Surfactant bilayers maintain transmembrane protein activity.Biophysical journal · 2014Article
- Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase.Biophysical journal · 2014Article
- Solid state NMR: The essential technology for helical membrane protein structural characterization.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Host Lipid and Temperature as Important Screening Variables for Crystallizing Integral Membrane Proteins in Lipidic Mesophases. Trials with Diacylglycerol Kinase.Crystal growth & design · 2013Article
- Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes.Biochemistry · 2012Article
- Characterization of lipid matrices for membrane protein crystallization by high-throughput small angle X-ray scattering.Methods (San Diego, Calif.) · 2011Article
- Lipidic cubic phase technologies for membrane protein structural studies.Current opinion in structural biology · 2011Review
- Crystallizing membrane proteins for structure-function studies using lipidic mesophases.Biochemical Society transactions · 2011Article
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3 authors.
Funding
Abstract
Structure determination of membrane proteins by crystallographic means has been facilitated by crystallization in lipidic mesophases. It has been suggested, however, that this so-called in meso method, as originally implemented, would not apply to small protein targets having </=4 transmembrane crossings. In our study, the hypothesis that the inherent flexibility of the mesophase would enable crystallogenesis of small proteins was tested using a transmembrane pentadecapeptide, linear gramicidin, which produced structure-grade crystals. This result suggests that the in meso method should be considered as a viable means for high-resolution structure determination of integral membrane peptides, many of which are predicted to be coded for in the human genome.
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