Search results for "complex assembly"

showing 2 items of 2 documents

Assembly of Spinach Chloroplast ATP Synthase Rotor Ring Protein-Lipid Complex

2019

Rotor ATPases are large multisubunit membrane protein complexes found in all kingdoms of life. The membrane parts of these ATPases include a ring-like assembly, so-called c-ring, consisting of several subunits c, plugged by a patch of phospholipids. In this report, we use a nature-inspired approach to model the assembly of the spinach (Spinacia oleracea) c14 ring protein-lipid complex, where partially assembled oligomers are pulled toward each other using a biasing potential. The resulting assemblies contain 23 to 26 encapsulated plug lipids, general position of which corresponds well to experimental maps. However, best fit to experimental data is achieved with 15 to 17 lipids inside the c-…

0301 basic medicineSpinaciaATPaseProtein subunitlipiditBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrysolukalvotprotein-lipid interactions03 medical and health sciences0302 clinical medicinecomplex assemblymembrane insertionMolecular Biosciencesmembrane proteinProtein–lipid interactionlcsh:QH301-705.5Molecular BiologyOriginal ResearchbiologyATP synthaseannular lipidsChemistrybiology.organism_classificationadenosiinitrifosfaatti030104 developmental biologyMembranelcsh:Biology (General)Membrane proteinProtein-lipid complex030220 oncology & carcinogenesisbiology.proteinBiophysicslipids (amino acids peptides and proteins)proteiinitFrontiers in Molecular Biosciences
researchProduct

Identification of SNARE complex modulators that inhibit exocytosis from an alpha-helix-constrained combinatorial library.

2003

Synthetic peptides patterned after the proteins involved in vesicle fusion [the so-called SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) proteins] are potent inhibitors of SNARE complex assembly and neuronal exocytosis. It is noteworthy that the identification of peptide sequences not related to the SNARE proteins has not been accomplished yet; this is due, in part, to the structural constraints and the specificity of the protein interactions that govern the formation of the SNARE complex. Here we have addressed this question and used a combinatorial approach to identify peptides that modulate the assembly of the SNARE core complex and inhibit neuronal…

Models MolecularVesicle fusionMacromolecular SubstancesChromaffin CellsMolecular Sequence DataVesicular Transport ProteinsBiologyBiochemistryExocytosisExocytosisProtein Structure SecondaryPeptide LibraryAnimalsAmino Acid SequencePeptide libraryMolecular BiologyCells CulturedSNARE complex assemblyNeuronsSTX1AMembrane ProteinsMunc-18Cell BiologyFusion proteinCell biologyRatsCattleSNARE complexPeptidesSNARE ProteinsResearch ArticleThe Biochemical journal
researchProduct