Search results for "TRANSMEMBRANE PROTEIN"

showing 10 items of 186 documents

A minimal hydrophobicity is needed to employ amphiphilic p(HPMA)-co-p(LMA) random copolymers in membrane research.

2014

Because a polymer environment might be milder than a detergent micelle, amphiphilic polymers have attracted attention as alternatives to detergents in membrane biochemistry. The polymer poly[N-(2-hydroxypropyl)-methacrylamid] [p(HPMA)] has recently been modified with hydrophobic lauryl methacrylate (LMA) moieties, resulting in the synthesis of amphiphilic p(HPMA)-co-p(LMA) polymers. p(HPMA)-co-p(LMA) polymers with a LMA content of 5 or 15% have unstable hydrophobic cores. This, on one hand, promotes interactions of the hydrophobic LMA moieties with membranes, resulting in membrane rupture, but at the same time prevents formation of a hydrophobic, membrane mimetic environment that is suffici…

chemistry.chemical_classificationChemistryPolymersMembrane lipidsPolymerBiochemistryTransmembrane proteinHydrophobic effectMembraneMembrane proteinAmphiphilePolymer chemistryCopolymerMethacrylatesHydrophobic and Hydrophilic InteractionsBiochemistry
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From Hydrophobic Matching to Interfacial Tuning: New Ideas for the Mutual Adaptation Between Membranes and Peptides

2009

It is widely accepted that membrane proteins and lipid bilayers are complementary in terms of the distribution in space of their hydrophobic and polar regions. Similarly, it is also accepted that the hydrophobic parts of the protein and the membrane must adapt to each other. Classically these ideas are rationalized under the concept of hydrophobic matching, which predicts a number of possible mechanisms by which proteins can vary their effective hydrophobic length, or membranes can change their hydrophobic thickness. Such effects have been studied in detail for simplified systems, like transmembrane peptides or protein fragments, which generally show that optimizing peptide orientation is t…

chemistry.chemical_classificationCrystallographyMembraneMembrane proteinchemistryChemical physicsOrientation (geometry)BilayerBiophysicsAnchoringPeptideLipid bilayerTransmembrane proteinBiophysical Journal
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Thermodynamics of the interaction between the spike protein of severe acute respiratory syndrome- coronavirus-2 and the receptor of human angiotensin…

2020

Since the end of 2019, the coronavirus SARS-CoV-2 has caused more than 180,000 deaths all over the world, still lacking a medical treatment despite the concerns of the whole scientific community. Human Angiotensin-Converting Enzyme 2 (ACE2) was recently recognized as the transmembrane protein serving as SARS-CoV-2 entry point into cells, thus constituting the first biomolecular event leading to COVID-19 disease. Here, by means of a state-of-the-art computational approach, we propose a rational evaluation of the molecular mechanisms behind the formation of the complex and of the effects of possible ligands. Moreover, binding free energy between ACE2 and the active Receptor Binding Domain (RB…

chemistry.chemical_classificationEnzymechemistrySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Angiotensin-converting enzyme 2medicineSpike ProteinComputational biologymedicine.disease_causeReceptorTransmembrane proteinCoronavirusProtein–protein interaction
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Self-Assembling of Peptide/Membrane Complexes by Atomistic Molecular Dynamics Simulations

2007

Abstract Model biological membranes consisting of peptide/lipid-bilayer complexes can nowadays be studied by classical molecular dynamics (MD) simulations at atomic detail. In most cases, the simulation starts with an assumed state of a peptide in a preformed bilayer, from which equilibrium configurations are difficult to obtain due to a relatively slow molecular diffusion. As an alternative, we propose an extension of reported work on the self-organization of unordered lipids into bilayers, consisting of including a peptide molecule in the initial random configuration to obtain a membrane-bound peptide simultaneous to the formation of the lipid bilayer. This strategy takes advantage of the…

chemistry.chemical_classificationModels MolecularMolecular diffusionMembranesChemistryMacromolecular SubstancesMembrane FluidityBilayerLipid BilayersMolecular ConformationBiophysicsPeptideBiological membraneTransmembrane proteinMolecular dynamicsCrystallographyMembraneModels ChemicalQuantum TheoryComputer SimulationLipid bilayerPeptidesPhospholipidsBiophysical Journal
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Intra-Helical Salt Bridge Contribution to Membrane Protein Insertion.

2021

ABSTRACTSalt bridges between negatively (D, E) and positively charged (K, R, H) amino acids play an important role in protein stabilization. This has a more prevalent effect in membrane proteins where polar amino acids are exposed to a very hydrophobic environment. In transmembrane (TM) helices the presence of charged residues can hinder the insertion of the helices into the membrane. This can sometimes be avoided by TM region rearrangements after insertion, but it is also possible that the formation of salt bridges could decrease the cost of membrane integration. However, the presence of intra-helical salt bridges in TM domains and their effect on insertion has not been properly studied ye…

chemistry.chemical_classificationProtein Conformation alpha-HelicalCell MembraneStatic ElectricityMembrane ProteinsElectrostaticsTransmembrane proteinAmino acidMembraneMembrane proteinchemistryStructural BiologyBiophysicsSalt bridgeProtein stabilizationAmino AcidsMolecular BiologyHydrophobic and Hydrophilic InteractionsBiogenesisJournal of molecular biology
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Carotenoids and the Assembly of Light-harvesting Complexes

2006

Carotenoids are constitutive components of all light-harvesting complexes in plants and many such complexes in bacteria. In the crystal structures of several light-harvesting complexes, carotenoids are seen to span the lipid bilayer and connect components of the complex on both membrane surfaces and/or to mediate the interaction of transmembrane protein helices. This important stabilizing function suggests that these pigments are also actively involved in the assembly of light-harvesting complexes. Verification of this notion appears too ambitious a goal at present, as the question of how the pigment-protein complexes of the photosynthetic apparatus are assembled is still open. However, inf…

chemistry.chemical_classificationbiologyChemistryorganic chemicalsfood and beveragesmacromolecular substancesbiology.organism_classificationPhotosynthesisbiological factorsTransmembrane proteinLight-harvesting complexRhodobacter sphaeroidesBiochemistrypolycyclic compoundsLipid bilayerCarotenoidBiogenesisFunction (biology)
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The hedgehog receptor patched is involved in cholesterol transport.

2011

International audience; BACKGROUND: Sonic hedgehog (Shh) signaling plays a crucial role in growth and patterning during embryonic development, and also in stem cell maintenance and tissue regeneration in adults. Aberrant Shh pathway activation is involved in the development of many tumors, and one of the most affected Shh signaling steps found in these tumors is the regulation of the signaling receptor Smoothened by the Shh receptor Patched. In the present work, we investigated Patched activity and the mechanism by which Patched inhibits Smoothened. METHODOLOGY/PRINCIPAL FINDINGS: Using the well-known Shh-responding cell line of mouse fibroblasts NIH 3T3, we first observed that enhancement …

ciliumlcsh:MedicineyeastBiochemistryReceptors G-Protein-CoupledTransmembrane Transport ProteinsMicechemistry.chemical_compound0302 clinical medicineMolecular Cell Biology[SDV.IDA]Life Sciences [q-bio]/Food engineeringMembrane Receptor SignalingBiomacromolecule-Ligand InteractionsSonic hedgehoglcsh:ScienceComputingMilieux_MISCELLANEOUS0303 health sciencesMultidisciplinaryMechanisms of Signal TransductionVeratrum Alkaloids[SDV.IDA] Life Sciences [q-bio]/Food engineeringdrosophilaSmoothened ReceptorLipidsHedgehog signaling pathwayCell biologySterolsSmoothened ReceptorAlimentation et Nutritionembryonic structurescilMembranes and Sorting[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Signal transductionvesicular traffickingSignal TransductionResearch Articleprimary ciliumPatched ReceptorsPatchedsignal-transductionanimal structuresCyclopamine[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringBiophysicsReceptors Cell Surfacepathway activationSaccharomyces cerevisiaetransduction du signalBiology03 medical and health sciencessonic hedgehoglipidAnimalsHumansFood and NutritionHedgehog Proteins[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringBiology030304 developmental biologyPatched Receptorsprotein signalsCell Membranelcsh:RProteinscholesterolBiological TransportTransmembrane Proteinssterol-sensing domainchemistry[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]NIH 3T3 Cellscholesterol;lipid;cell trafficking; yeast;drosophila;cells ; pathway activation; vesicular trafficking; signal-transduction; sonic hedgehog;sterol-sensing domain; primary cilium;protein signalsbiology.proteincellslcsh:Qcell traffickingSmoothened030217 neurology & neurosurgery
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Investigating REPAIRv2 as a Tool to Edit CFTR mRNA with Premature Stop Codons

2020

Cystic fibrosis (CF) is caused by mutations in the gene encoding the transmembrane conductance regulator (CFTR) protein. Some CF patients are compound heterozygous or homozygous for nonsense mutations in the CFTR gene. This implies the presence in the transcript of premature termination codons (PTCs) responsible for a truncated CFTR protein and a more severe form of the disease. Aminoglycoside and PTC124 derivatives have been used for the read-through of PTCs to restore the full-length CFTR protein. However, in a precision medicine framework, the CRISPR/dCas13b-based molecular tool &ldquo

congenital hereditary and neonatal diseases and abnormalitiesRNA editingMutantNonsense mutationSettore BIO/11 - Biologia MolecolareBiologyCRISPR/dCas13bCatalysislcsh:Chemistrycystic fibrosisInorganic ChemistryGuide RNASettore BIO/06 - Anatomia Comparata E CitologiaPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologyGeneSpectroscopyMessenger RNApremature termination codons (PTCs)Organic ChemistryGeneral Medicinerespiratory systemStop codonTransmembrane proteinrespiratory tract diseasesComputer Science ApplicationsCell biologySettore BIO/18 - Geneticalcsh:Biology (General)lcsh:QD1-999RNA editingInternational Journal of Molecular Sciences
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Induced Night-Vision by Singlet-Oxygen-Mediated Activation of Rhodopsin

2019

In humans, vision is limited to a small fraction of the whole electromagnetic spectrum. One possible strategy for enhancing vision in deep-red or poor-light conditions consists of recruiting chlorophyll derivatives in the rod photoreceptor cells of the eye, as suggested in the case of some deep-sea fish. Here, we employ all-atom molecular simulations and high-level quantum chemistry calculations to rationalize how chlorin e6 (Ce6), widely used in photodynamic therapy although accompanied by enhanced visual sensitivity, mediates vision in the dark, shining light on a fascinating but largely unknown molecular mechanism. First, we identify persistent interaction sites between Ce6 and the extra…

genetic structuresbiology010405 organic chemistrySinglet oxygenPhotoreceptor proteinRetinal010402 general chemistry01 natural sciencesVisual sensitivityeye diseasesTransmembrane protein0104 chemical scienceschemistry.chemical_compoundchemistryRhodopsinNight visionbiology.proteinBiophysics[CHIM]Chemical SciencesGeneral Materials SciencePhysical and Theoretical ChemistryComputingMilieux_MISCELLANEOUSVisual phototransduction
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Viroporins, Examples of the Two-Stage Membrane Protein Folding Model

2015

Viroporins are small, α-helical, hydrophobic virus encoded proteins, engineered to form homo-oligomeric hydrophilic pores in the host membrane. Viroporins participate in multiple steps of the viral life cycle, from entry to budding. As any other membrane protein, viroporins have to find the way to bury their hydrophobic regions into the lipid bilayer. Once within the membrane, the hydrophobic helices of viroporins interact with each other to form higher ordered structures required to correctly perform their porating activities. This two-step process resembles the two-stage model proposed for membrane protein folding by Engelman and Poppot. In this review we use the membrane protein folding …

influenza A virus M2Protein Foldingviroporinslcsh:QR1-502ReviewBiologyhelix-helix packinglcsh:MicrobiologyCell membraneViral ProteinsVirologymedicinetransmembrane protein foldingAnimalsHumansmembrane insertionLipid bilayerCell MembraneVirologyTransmembrane proteinVirusFolding (chemistry)Transmembrane domainGenòmicaInfectious DiseasesMembranemedicine.anatomical_structureMembrane proteinVirus DiseasesVirusesBiophysicsProtein foldingProteïnesGenètica
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