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1. Full Text Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
by Chorev, Dror S and Baker, Lindsay A and Wu, Di and Beilsten-Edmands, Victoria and Rouse, Sarah L and Zeev-Ben-Mordehai, Tzviya and Jiko, Chimari and Samsudin, Firdaus and Gerle, Christoph and Khalid, Syma and Stewart, Alastair G and Matthews, Stephen J and Grünewald, Kay and Robinson, Carol V
Science, ISSN 0036-8075, 11/2018, Volume 362, Issue 6416, pp. 829 - 834
Membrane proteins reside in lipid bilayers and are typically extracted from this environment for study, which often compromises their integrity. In this work,... 
OUTER-MEMBRANE | NMR | OXIDASE | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | LIPIDS | SUBUNIT | Molecular Chaperones - metabolism | Bacterial Proteins - chemistry | Porins - metabolism | Molecular Chaperones - chemistry | Proteome - chemistry | Adenine Nucleotide Translocator 1 - chemistry | Cattle | Mass Spectrometry | Mitochondrial Membranes - chemistry | Porins - chemistry | Membrane Proteins - metabolism | SEC Translocation Channels - chemistry | SEC Translocation Channels - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Adenine Nucleotide Translocator 1 - metabolism | Mitochondrial Proton-Translocating ATPases - chemistry | Mitochondrial Proton-Translocating ATPases - metabolism | Mitochondrial Membranes - metabolism | Animals | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Protein Conformation, beta-Strand | Bacterial Proteins - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli Proteins - chemistry | Proteome - metabolism | Physiological aspects | Mass spectrometry | Methods | Membrane proteins | Escherichia coli | Muscle proteins | Fatty acids | Porins | Adenosine triphosphate | Adenosine triphosphatase | Stoichiometry | Membranes | Outer membranes | Lipids | Translocase | Chaperones | ADP | Lipid bilayers | Proteins | Mitochondria | E coli | Bacteria | Assemblies | Efflux | Inner membranes | Adenosine | Adenosine diphosphate | Membrane vesicles | Mass spectroscopy | Electron microscopy | Organic chemistry | Scientific imaging | Dimers | Disruption | ATP | Ejection | Index Medicus
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2. Full Text Asymmetric droplet interface bilayers
by Hwang, William L and Chen, Min and Cronin, Bríd and Holden, Matthew A and Bayley, Hagan
Journal of the American Chemical Society, ISSN 0002-7863, 05/2008, Volume 130, Issue 18, pp. 5878 - 5879
In cell membranes, the lipid compositions of the inner and outer leaflets differ. Therefore, a robust model system that enables single-channel electrical... 
OMPG | LIPID-BILAYERS | MONOMERIC PORIN | VESICLES | MEMBRANES | PHOSPHOLIPIDS | CHEMISTRY, MULTIDISCIPLINARY | MONOLAYERS | Lipids - chemistry | Membrane Proteins - chemistry | Solutions | Water - chemistry | Bacterial Outer Membrane Proteins - chemistry | Porins - chemistry | Lipid Bilayers - chemistry | Escherichia coli Proteins - chemistry | Alkanes - chemistry | Ion Channels - chemistry | Lipid membranes | Composition | Usage | Diffraction | X-rays | Nuclear magnetic resonance spectroscopy | Structure | Index Medicus
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3. Full Text Transport across the outer membrane porin of mycolic acid containing actinomycetales: Nocardia farcinica
by Singh, Pratik Raj and Bajaj, Harsha and Benz, Roland and Winterhalter, Mathias and Mahendran, Kozhinjampara R
BBA - Biomembranes, ISSN 0005-2736, 02/2015, Volume 1848, Issue 2, pp. 654 - 661
The role of the outer-membrane channel from a mycolic acid containing Gram-positive bacteria , which forms a hydrophilic pathway across the cell wall, was... 
Mycolata | Porin | Nocardia farcinica | Single channel electrophysiology | Antibiotic resistance | TRANSLOCATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MYCOBACTERIUM-SMEGMATIS | CELL-WALL | BIOPHYSICS | CHANNEL | OMPF PORIN | RESISTANCE | BETA-LACTAM ANTIBIOTICS | PERMEABILITY BARRIER | MOLECULAR-BASIS | Nocardia - chemistry | Bacterial Proteins - chemistry | Porins - metabolism | Cell Membrane - chemistry | Biological Transport | Anti-Bacterial Agents - chemistry | Escherichia coli - metabolism | Porins - chemistry | Cell Membrane - metabolism | Recombinant Proteins - metabolism | Gene Expression | Mutagenesis, Site-Directed | Porins - genetics | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Cell Wall - chemistry | Static Electricity | Mycolic Acids - chemistry | beta-Lactams - chemistry | Nocardia - metabolism | Amikacin - chemistry | Liposomes - chemistry | Escherichia coli - genetics | Hydrophobic and Hydrophilic Interactions | Bacterial Proteins - metabolism | Kanamycin - chemistry | Structural Homology, Protein | Mutation | Antibacterial agents | Porins
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4. Full Text PoreDesigner for tuning solute selectivity in a robust and highly permeable outer membrane pore
by Chowdhury, Ratul and Ren, Tingwei and Shankla, Manish and Decker, Karl and Grisewood, Matthew and Prabhakar, Jeevan and Baker, Carol and Golbeck, John H and Aksimentiev, Aleksei and Kumar, Manish and Maranas, Costas D
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 3661 - 10
Monodispersed angstrom-size pores embedded in a suitable matrix are promising for highly selective membrane-based separations. They can provide substantial... 
MOLECULAR-DYNAMICS | DE-NOVO DESIGN | OMPF PORIN | MULTIDISCIPLINARY SCIENCES | X-RAY-STRUCTURE | PURIFICATION | AQUAPORIN WATER CHANNELS | LIGHT-SCATTERING | MECHANISMS | PROTEINS | PERMEATION | Protein Engineering - methods | Aquaporins - chemistry | Osmosis | Permeability | Escherichia coli - chemistry | Molecular Dynamics Simulation | Aquaporin 1 - chemistry | Cell Membrane - chemistry | Thermodynamics | Membrane Proteins - chemistry | Solutions | Models, Biological | Water - chemistry | Porins - chemistry | Mutation | Sodium Chloride - chemistry | Water treatment | Channel pores | Membranes | Water chemistry | Sucrose | Aquaporins | Water conservation | Workflow | Solutes | Selectivity | Redesign | Membrane proteins | Proteins | Organic chemistry | Design engineering | Pore size | Energy conservation | Biological membranes | Pores | Porosity | Sugars | Index Medicus
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5. Full Text The PnrA (Tp0319; TmpC) Lipoprotein Represents a New Family of Bacterial Purine Nucleoside Receptor Encoded within an ATP-binding Cassette (ABC)-like Operon in Treponema pallidum
by Ranjit K. Deka and Chad A. Brautigam and Xiaofeng F. Yang and Jon S. Blevins and Mischa Machius and Diana R. Tomchick and Michael V. Norgard and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Journal of Biological Chemistry, ISSN 0021-9258, 03/2006, Volume 281, Issue 12, pp. 8072 - 8081
Treponema pallidum , the bacterial agent of syphilis, cannot be cultivated in vitro . This constraint has severely impeded the study of the membrane biology of... 
SYPHILIS SPIROCHETE | PERIPLASMIC LYSINE | BORRELIA-BURGDORFERI LIPOPROTEINS | OUTER-MEMBRANE PROTEIN | SUBSP PALLIDUM | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | X-RAY STRUCTURE | CRYSTALLOGRAPHY | PORIN ACTIVITY | LIGAND | Models, Chemical | Humans | Open Reading Frames | Bacterial Proteins - chemistry | Crystallography, X-Ray | Cytoplasm - metabolism | DNA Primers - chemistry | Biological Transport | Time Factors | Cloning, Molecular | Escherichia coli - metabolism | Lipoproteins - metabolism | Transcription, Genetic | Cell Membrane - metabolism | Binding Sites | Protein Structure, Tertiary | Genes, Bacterial | Rabbits | Nucleosides - chemistry | Protein Structure, Secondary | Treponema pallidum - metabolism | Models, Molecular | Recombinant Proteins - chemistry | RNA - chemistry | Reverse Transcriptase Polymerase Chain Reaction | Membrane Proteins | Animals | Purines - chemistry | Protein Binding | Calorimetry | Ligands | Kinetics | Proteins - chemistry | Adenosine Triphosphate - chemistry | Histidine - chemistry | Index Medicus
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6. Full Text Discovery of a Kojibiose Phosphorylase in Escherichia coli K-12
by Mukherjee, Keya and Narindoshvili, Tamari and Raushel, Frank M
Biochemistry, ISSN 0006-2960, 05/2018, Volume 57, Issue 19, pp. 2857 - 2867
The substrate profiles for three uncharacterized enzymes (YcjM, YcjT, and YcjU) that are expressed from a cluster of 12 genes (ycjM-W and ompG) of unknown... 
THERMOANAEROBACTER-BROCKII | SUCROSE PHOSPHORYLASE | COMPATIBLE SOLUTE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-GLUCOSIDASE | GUT MICROBIOTA | GLUCOSIDASE-I | BETA-PHOSPHOGLUCOMUTASE | PORIN PROTEIN | MAJOR OSMOTIC SOLUTES | Porins - genetics | Bacterial Outer Membrane Proteins - chemistry | Substrate Specificity | Teichoic Acids - chemistry | Disaccharides - chemistry | Mannosephosphates - chemistry | Glucose - chemistry | Glucosyltransferases - chemistry | Escherichia coli Proteins - genetics | Porins - chemistry | Lipopolysaccharides - chemistry | Catalysis | Kinetics | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Glucosyltransferases - classification | Bacterial Outer Membrane Proteins - genetics | Escherichia coli K12 - enzymology | Glucosyltransferases - genetics | Escherichia coli | Isomerization | Analysis | Genetic aspects | Research | Gene expression | Phosphorylase | Index Medicus
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7. Full Text Semisynthetic protein nanoreactor for single-molecule chemistry
by Joongoo Lee and Hagan Bayley
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2015, Volume 112, Issue 45, pp. 13768 - 13773
The covalent chemistry of individual reactants bound within a protein pore can be monitored by observing the ionic current flow through the pore, which acts as... 
semisynthesis | STOCHASTIC DETECTION | single-molecule chemistry | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | NATIVE CHEMICAL LIGATION | click chemistry | LEVEL | NANOPORE | STAPHYLOCOCCAL ALPHA-HEMOLYSIN | COVALENT CHEMISTRY | ADAPTER | PORE-FORMING PROTEIN | alpha-hemolysin | Protein Engineering - methods | Nanotechnology - methods | Electrophoresis, Polyacrylamide Gel | Click Chemistry - methods | Models, Molecular | Alkynes - chemistry | DNA Primers - genetics | Azides - chemistry | Molecular Dynamics Simulation | Mass Spectrometry | Chromatography, Liquid | Porins - chemistry | Chromatography, Gel | Copper | Porins - biosynthesis | Usage | Polypeptides | Ligases | Amino acids | Nucleotide sequencing | Research | DNA sequencing | Proteins | Molecules | Peptides | Chemical bonds | Chemical reactions | Molecular chemistry | Index Medicus | Biological Sciences | Physical Sciences
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8. Full Text The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition
by Hussain, Sunyia and Bernstein, Harris D
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2959 - 2973
Most proteins that reside in the bacterial outer membrane (OM) have a distinctive "beta-barrel" architecture, but the assembly of these proteins is poorly... 
IN-VITRO | GRAM-NEGATIVE BACTERIA | CONFORMATIONAL-CHANGES | BETA-BARREL | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | AUTOTRANSPORTER | BARREL ASSEMBLY MACHINERY | YAET COMPLEX | SECRETION | MOLECULAR-BASIS | Protein Multimerization | Porins - metabolism | Recombinant Fusion Proteins - metabolism | Lipid-Linked Proteins - metabolism | Escherichia coli - metabolism | Serine Endopeptidases - genetics | Porins - chemistry | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Bacterial Outer Membrane Proteins - genetics | Protein Conformation, alpha-Helical | Peptide Fragments - metabolism | Porins - genetics | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Serine Endopeptidases - chemistry | Recombinant Fusion Proteins - chemistry | Escherichia coli - chemistry | Protein Folding | Protein Transport | Peptide Fragments - chemistry | Bacterial Outer Membrane Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli Proteins - genetics | Serine Endopeptidases - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Liposomes | Escherichia coli Proteins - chemistry | Lipid-Linked Proteins - genetics | Lipid-Linked Proteins - chemistry | Index Medicus | outer membrane | molecular chaperone | beta-barrel proteins | Bam complex | protein-lipid interaction | Membrane Biology | membrane protein | protein folding | Gram-negative bacteria
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9. Full Text Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state mas nmr spectroscopy of large proteins
by Lalli, D and Schanda, P and Chowdhury, A and Retel, J and Hiller, M and Higman, V.A and Handel, L and Agarwal, V and Reif, B and Rossum, B. van and Akbey, U and Oschkinat, H
Journal of Biomolecular NMR, ISSN 0925-2738, 2011, Volume 51, Issue 4, pp. 477 - 485
Well-resolved 2H–13C correlation spectra, reminiscent of 1H–13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane... 
Biochemistry, general | Polymer Sciences | Ubiquitin | OmpG | Solid-state NMR | Micro-crystalline | Deuterium-carbon correlations | Biophysics and Biological Physics | Physics | Membrane proteins | ANGLE-SPINNING NMR | TRIPLE-RESONANCE NMR | CHEMICAL-SHIFTS | MAGNETIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ROTATING SOLIDS | SPECTROSCOPY | ASSIGNMENT | DYNAMICS | PERDEUTERATED PROTEINS | SPECTRA | DOUBLE-QUANTUM NMR | Carbon - metabolism | Deuterium - metabolism | Humans | Porins - metabolism | Ubiquitin - chemistry | Ubiquitin - metabolism | Bacterial Outer Membrane Proteins - chemistry | Deuterium - chemistry | Escherichia coli Proteins - metabolism | Escherichia coli - cytology | Hydrogen - chemistry | Carbon - chemistry | Isotope Labeling - methods | Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Nuclear Magnetic Resonance, Biomolecular - methods | Escherichia coli - metabolism | Porins - chemistry | Proteins - chemistry | Escherichia coli Proteins - chemistry | Hydrogen - metabolism | Nuclear magnetic resonance spectroscopy | Amino acids | Index Medicus
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10. Full Text Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex
by Ellisdon, Andrew M and Dimitrova, Lyudmila and Hurt, Ed and Stewart, Murray
Nature Structural and Molecular Biology, ISSN 1545-9993, 03/2012, Volume 19, Issue 3, pp. 328 - 336
The conserved TREX-2 transcription-export complex integrates transcription and processing of many actively transcribed nascent mRNAs with the recruitment of... 
PERIPHERY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MACHINERY | MESSENGER-RNA EXPORT | SACCHAROMYCES-CEREVISIAE | PROCESSING FACTORS | PROTEIN COMPLEX | CELL BIOLOGY | BIOPHYSICS | ELONGATION | PROTEASOME | GENES | FUNCTIONAL COMPONENT | RNA-Binding Proteins - genetics | Humans | Porins - metabolism | Molecular Sequence Data | RNA, Messenger - metabolism | Cell Cycle Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Nucleocytoplasmic Transport Proteins - chemistry | Protein Structure, Quaternary | Cell Cycle Proteins - genetics | Conserved Sequence | Porins - chemistry | Ribonucleoproteins - genetics | Transcription, Genetic | Protein Stability | Ribonucleoproteins - chemistry | Nuclear Proteins - genetics | Calcium-Binding Proteins - chemistry | Calcium-Binding Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Porins - genetics | RNA Transport | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Nuclear Proteins - metabolism | Nucleic Acids - metabolism | Ribonucleoproteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | Nucleocytoplasmic Transport Proteins - genetics | Saccharomyces cerevisiae - chemistry | RNA, Fungal - metabolism | Proteasome Endopeptidase Complex - genetics | Sequence Alignment | Animals | Nucleocytoplasmic Transport Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Proteasome Endopeptidase Complex - metabolism | RNA-Binding Proteins - metabolism | Calcium-Binding Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Physiological aspects | Genetic aspects | Messenger RNA | Research | Gene mutations | Yeast fungi | Proteins | Yeast | Molecular biology | Ribonucleic acid--RNA | Gene expression | Genomics | Index Medicus
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11. Full Text The Nuclear Pore-Associated TREX-2 Complex Employs Mediator to Regulate Gene Expression
by Schneider, Maren and Hellerschmied, Doris and Schubert, Tobias and Amlacher, Stefan and Vinayachandran, Vinesh and Reja, Rohit and Pugh, B. Franklin and Clausen, Tim and Köhler, Alwin
Cell, ISSN 0092-8674, 08/2015, Volume 162, Issue 5, pp. 1016 - 1028
Nuclear pore complexes (NPCs) influence gene expression besides their established function in nuclear transport. The TREX-2 complex localizes to the NPC basket... 
RNA-POLYMERASE-II | YEAST | DISSOCIATION | PATHWAY | EXPORT MACHINERY | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | SACCHAROMYCES | ARCHITECTURE | PROTEINS | BINDING | CELL BIOLOGY | Mediator Complex - metabolism | Humans | Porins - metabolism | Transcriptome | Molecular Sequence Data | RNA Polymerase II - metabolism | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | X-Ray Diffraction | Nucleocytoplasmic Transport Proteins - chemistry | Porins - chemistry | Transcription, Genetic | Ribonucleoproteins - chemistry | Amino Acid Sequence | Promoter Regions, Genetic | Porins - genetics | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Ribonucleoproteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Nuclear Pore - metabolism | Nucleocytoplasmic Transport Proteins - genetics | Saccharomyces cerevisiae - chemistry | Multiprotein Complexes - chemistry | Sequence Alignment | Animals | Nucleocytoplasmic Transport Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Proteasome Endopeptidase Complex - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA | Molecular biology | Gene expression | Genes | Medicine, Experimental | Medical research | Messenger RNA | Genetic transcription | Index Medicus
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12. Full Text Nucleobase Recognition by Truncated α-Hemolysin Pores
by Ayub, Mariam and Stoddart, David and Bayley, Hagan
ACS Nano, ISSN 1936-0851, 08/2015, Volume 9, Issue 8, pp. 7895 - 7903
The alpha-hemolysin (alpha HL) protein nanopore has been investigated previously as a base detector for the strand sequencing of DNA and RNA. Recent findings... 
base identification | truncated pore | nanopore | toroidal lipid pore | alpha-hemolysin | SINGLE-MOLECULE | CYCLODEXTRIN | MATERIALS SCIENCE, MULTIDISCIPLINARY | CHEMISTRY, PHYSICAL | NANOSCIENCE & NANOTECHNOLOGY | CHEMISTRY, MULTIDISCIPLINARY | FORMING PROTEIN | BIOLOGICAL NANOPORE | OLIGONUCLEOTIDES | DISCRIMINATION | DNA | ADAPTER | PROTEIN NANOPORE | Protein Structure, Tertiary | Porins - genetics | Mycobacterium smegmatis - chemistry | Protein Structure, Secondary | Hemolysin Proteins - genetics | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - chemistry | Adenine - analysis | Recombinant Proteins - genetics | Hemolysin Proteins - chemistry | Static Electricity | Adenine - chemistry | Point Mutation | beta-Cyclodextrins - chemistry | Base Sequence | Poly C - analysis | Biosensing Techniques | Porins - chemistry | Lipid Bilayers - chemistry | Poly C - chemistry | Nanopores - ultrastructure | Amino Acid Substitution | Index Medicus | Charging | Deoxyribonucleic acid | Strands | Nucleosides | Lipids | Nanostructure | Porosity | Recognition
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13. Full Text Structural determinants of the hydrogen peroxide permeability of aquaporins
by Almasalmeh, Abdulnasser and Krenc, Dawid and Wu, Binghua and Beitz, Eric
FEBS Journal, ISSN 1742-464X, 2014, Volume 281, Issue 3, pp. 647 - 656
Aquaporins (AQP) conduct small, uncharged molecules, such as water (orthodox AQPs), ammonia (aquaammoniaporins) or glycerol (aquaglyceroporins). The... 
Water | Plasmodium falciparum | Hydrogen peroxide | Transport | Aquaporin | AQUAGLYCEROPORIN | AMMONIA | GLYCEROL | BIOCHEMISTRY & MOLECULAR BIOLOGY | hydrogen peroxide | WATER CHANNELS | transport | aquaporin | water | SACCHAROMYCES-CEREVISIAE | PLASMA-MEMBRANE | PLASMODIUM-FALCIPARUM | MEMBRANE-TRANSPORT | Oxidative Stress | Humans | Aquaporins - chemistry | Porins - metabolism | Cell Membrane Permeability | Protozoan Proteins - genetics | Aquaporin 1 - metabolism | Aquaporins - genetics | Protoplasts - metabolism | Protozoan Proteins - metabolism | Porins - chemistry | Plasmodium falciparum - metabolism | Protozoan Proteins - chemistry | Recombinant Proteins - metabolism | Porins - genetics | Water - metabolism | Rats | Recombinant Proteins - chemistry | Aquaporins - metabolism | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Hydrogen Peroxide - metabolism | Aquaporin 1 - chemistry | Aquaporin 1 - genetics | Point Mutation | Animals | Mutant Proteins - chemistry | Protein Isoforms | Protein Conformation | Kinetics | Amino Acid Substitution | Glycerin | Gene mutations | Malaria | Analysis | Aquaporins | Glycerol | Mitochondrial DNA | Permeability | Molecular chemistry | Cellular biology | Index Medicus
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14. Full Text Biomimetic Strategy to Reversibly Trigger Functionality of Catalytic Nanocompartments by the Insertion of pH-Responsive Biovalves
by Edlinger, Christoph and Einfalt, Tomaz and Spulber, Mariana and Car, Anja and Meier, Wolfgang and Palivan, Cornelia G
Nano Letters, ISSN 1530-6984, 09/2017, Volume 17, Issue 9, pp. 5790 - 5798
We describe an innovative strategy to generate catalytic compartments with triggered functionality at the nanoscale level by combining pH-reversible biovalves... 
triggered bioactivity | catalytic nanocompartment | membrane protein | reversible permeability | Stimuli responsiveness | PHYSICS, CONDENSED MATTER | PHYSICS, APPLIED | VESICLES | MATERIALS SCIENCE, MULTIDISCIPLINARY | ESCHERICHIA-COLI | LIGHT | CHEMISTRY, PHYSICAL | NANOSCIENCE & NANOTECHNOLOGY | SITE-DIRECTED MUTAGENESIS | CHEMISTRY, MULTIDISCIPLINARY | HYDROPHOBIC MISMATCH | OUTER-MEMBRANE PROTEIN | PROTEIN-POLYMER NANOREACTORS | ION CHANNELS | RECONSTITUTION | WATER | Amino Acid Sequence | Enzymes, Immobilized - chemistry | Peptides - chemistry | Membranes, Artificial | Models, Molecular | Delayed-Action Preparations - chemistry | Horseradish Peroxidase - administration & dosage | Permeability | Escherichia coli - chemistry | Horseradish Peroxidase - chemistry | Biomimetics | Porins - chemistry | Enzymes, Immobilized - administration & dosage | Polymers - chemistry | Catalysis | Hydrogen-Ion Concentration | Index Medicus
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