ArticleBiophysical journal2003
Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- Exploring protein-protein interactions and oligomerization state of pulmonary surfactant protein C (SP-C) through FRET and fluorescence self-quenching.Protein science : a publication of the Protein Society · 2024Article
- Hydrophobic matching controls the tilt and stability of the dimeric platelet-derived growth factor receptor (PDGFR) β transmembrane segment.The Journal of biological chemistry · 2012Article
- Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Cellular and molecular life sciences : CMLS · 2011Review
- Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.PloS one · 2011Article
- FRET in Membrane Biophysics: An Overview.Frontiers in physiology · 2011Article
- Transmembrane peptides influence the affinity of sterols for phospholipid bilayers.Biophysical journal · 2010Article
- Viruses: incredible nanomachines. New advances with filamentous phages.European biophysics journal : EBJ · 2010Review
- Membrane microheterogeneity: Förster resonance energy transfer characterization of lateral membrane domains.European biophysics journal : EBJ · 2010Review
- Clustering and lateral concentration of raft lipids by the MAL protein.Molecular biology of the cell · 2009Article
- Membrane protein frustration: protein incorporation into hydrophobic mismatched binary lipid mixtures.Biophysical journal · 2009Article
- Site-directed fluorescence labeling of a membrane protein with BADAN: probing protein topology and local environment.Biophysical journal · 2008Article
- Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress.Biophysical journal · 2007Article
- FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein.Biophysical journal · 2007Article
- The dynamin middle domain is critical for tetramerization and higher-order self-assembly.The EMBO journal · 2007Article
- Motional restrictions of membrane proteins: a site-directed spin labeling study.Biophysical journal · 2006Article
- FRET study of membrane proteins: simulation-based fitting for analysis of membrane protein embedment and association.Biophysical journal · 2006Article
- Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins.Biophysical journal · 2005Article
- Lipid bilayer topology of the transmembrane alpha-helix of M13 Major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy.Biophysical journal · 2004Article
- Quantification of Protein-Lipid Selectivity using FRET: Application to the M13 Major Coat Protein.Biophysical journal · 2004Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
M13 major coat protein was derivatized with BODIPY (n-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-yl)methyl iodoacetamide), and its aggregation was studied in 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and DOPC/1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (DOPG) or 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE)/DOPG (model systems of membranes with hydrophobic thickness matching that of the protein) using photophysical methodologies (time-resolved and steady-state self-quenching, absorption, and emission spectra). It was concluded that the protein is essentially monomeric, even in the absence of anionic phospholipids. The protein was also incorporated in pure bilayers of lipids with a strong mismatch with the protein transmembrane length, 1,2-dierucoyl-sn-glycero-3-phosphocholine (DEuPC, longer lipid) and 1,2-dimyristoleoyl-sn-glycero-3-phosphocholine (DMoPC, shorter lipid), and in lipidic mixtures containing DOPC and one of these lipids. The protein was aggregated in the pure vesicles of mismatching lipid but remained essentially monomeric in the mixtures as detected from BODIPY fluorescence emission self-quenching. From fluorescence resonance energy transfer (FRET) measurements (donor-n-(iodoacetyl)aminoethyl-1-sulfonaphthylamine (IAEDANS)-labeled protein; acceptor-BODIPY labeled protein), it was concluded that in the DEuPC/DOPC and DMoPC/DOPC lipid mixtures, domains enriched in the protein and the matching lipid (DOPC) are formed.
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