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1. Full Text Membrane proteins bind lipids selectively to modulate their structure and function
by Laganowsky, Arthur and Reading, Eamonn and Allison, Timothy M and Ulmschneider, Martin B and Degiacomi, Matteo T and Baldwin, Andrew J and Robinson, Carol V
Nature, ISSN 0028-0836, 2014, Volume 510, Issue 7503, pp. 172 - 175
Previous studies have established that the folding, structure and function of membrane proteins are influenced by their lipid environments(1-7) and that lipids... 
MYCOBACTERIUM-TUBERCULOSIS | ATOM FORCE-FIELD | MOLECULAR-DYNAMICS | MULTIDISCIPLINARY SCIENCES | COMPLEXES | PURIFICATION | ION-CHANNEL | MOBILITY-MASS SPECTROMETRY | MODEL | MSCL | WATER | Apoproteins - chemistry | Cardiolipins - pharmacology | Protein Unfolding - drug effects | Protein Conformation - drug effects | Aquaporins - chemistry | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Membrane Lipids - chemistry | Cation Transport Proteins - metabolism | Protein Folding - drug effects | Mass Spectrometry | Mycobacterium tuberculosis - chemistry | Membrane Proteins - metabolism | Ion Channels - chemistry | Phosphatidylglycerols - metabolism | Apoproteins - metabolism | Ammonia - metabolism | Models, Molecular | Aquaporins - metabolism | Escherichia coli Proteins - metabolism | Cardiolipins - metabolism | Escherichia coli - chemistry | Cardiolipins - chemistry | Phosphatidylglycerols - chemistry | Ion Channels - metabolism | Membrane Proteins - chemistry | Protein Stability - drug effects | Membrane Lipids - metabolism | Phosphatidylglycerols - pharmacology | Bacterial Proteins - metabolism | Membrane Lipids - pharmacology | Lipid Bilayers - chemistry | Cation Transport Proteins - chemistry | Escherichia coli Proteins - chemistry | Biological research | Physiological aspects | Lipids | Cooperative binding (Biochemistry) | Research | Structure | Molecular biology | Membrane proteins | Biology, Experimental | Proteins | Studies | Membranes | E coli | Binding sites | Crystal structure | Index Medicus
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2. Full Text Mechanism of Selectivity in Aquaporins and Aquaglyceroporins
by Jochen S. Hub and Bert L. de Groot
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2008, Volume 105, Issue 4, pp. 1198 - 1203
Aquaporins and aquaglyceroporins form a family of pore proteins that facilitate the efficient and selective flux of small solutes across biological membranes.... 
Molecules | Ammonia | Hydrogen bonds | Aquaglyceroporins | Aquaporins | Molecular interactions | Atoms | Umbrellas | Solutes | Hydrophobicity | Membrane permeation | Potential of mean force | Molecular dynamics simulations | Free-energy profile | Umbrella sampling | molecular dynamics simulations | free-energy profile | umbrella sampling | MOLECULAR-DYNAMICS | GLYCEROL FACILITATOR | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | PARTICLE MESH EWALD | LIPID BILAYER-MEMBRANES | STRUCTURAL DETERMINANTS | potential of mean force | XENOPUS-OOCYTES | FORCE-FIELD | WATER CHANNEL | membrane permeation | CELL CHIP28 PROTEIN | Carbon Dioxide - chemistry | Computational Biology - methods | Humans | Aquaporins - chemistry | Permeability | Aquaglyceroporins - chemistry | Urea - chemistry | Aquaporin 1 - chemistry | Aquaporin 1 - genetics | Point Mutation | Thermodynamics | Animals | Solutions | Cattle | Oxygen - chemistry | Water - chemistry | Hydrophobic and Hydrophilic Interactions | Signal Transduction - physiology | Ammonia - chemistry | Lipid Bilayers - chemistry | Escherichia coli Proteins - chemistry | Glycerol - chemistry | Molecular dynamics | Hydrophobic effect | Research | Properties | Proteins | Studies | Membranes | Molecular biology | Solute movement | Index Medicus | Biological Sciences
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3. Full Text Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants
by Yaghmur, Anan and Laggner, Peter and Zhang, Shuguang and Rappolt, Michael
PLoS ONE, ISSN 1932-6203, 05/2007, Volume 2, Issue 5, pp. e479 - e479
This study reports the effect of loading four different charged designer lipid-like short anionic and cationic peptide surfactants on the fully hydrated... 
BIOLOGY | Anions | Lipids - chemistry | Temperature | Lipid Bilayers | Peptides - chemistry | Models, Molecular | Scattering, Radiation | Surface-Active Agents - chemistry | Aspartate | Peptides | Surface active agents | Aquaporins | Membranes | Molecular structure | Hydrocarbons | Amino acids | Lipids | Biochemistry | Hydrophobicity | Small angle X ray scattering | Lipid bilayers | X-ray scattering | E coli | Aspartic acid | Hexagonal phase | Pollutants | Surface activity | Alanine | Stability | Hydration | Cationic peptides | Biophysics | Surfactants | Studies | Acids | Lysine | X ray scattering | Cations | Curvature | Index Medicus
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4. Full Text Lipid–protein nanodiscs promote in vitro folding of transmembrane domains of multi-helical and multimeric membrane proteins
by Shenkarev, Zakhar O and Lyukmanova, Ekaterina N and Butenko, Ivan O and Petrovskaya, Lada E and Paramonov, Alexander S and Shulepko, Mikhail A and Nekrasova, Oksana V and Kirpichnikov, Mikhail P and Arseniev, Alexander S
BBA - Biomembranes, ISSN 0005-2736, 02/2013, Volume 1828, Issue 2, pp. 776 - 784
Production of helical integral membrane proteins (IMPs) in a folded state is a necessary prerequisite for their functional and structural studies. In many... 
Membrane protein folding | Reconstructed high-density lipoprotein | Bacteriorhodopsin ESR | Potassium channel KcsA | Membrane mimetic | Cell-free expression | PHOSPHOLIPID-BILAYER NANODISCS | FULL-LENGTH KCSA | BIOCHEMISTRY & MOLECULAR BIOLOGY | KCSA POTASSIUM CHANNEL | DETERGENT MICELLES | DENATURED STATE | NMR | BIOPHYSICS | NANOLIPOPROTEIN PARTICLES | K+ CHANNEL | BACTERIORHODOPSIN | EXPRESSION | Protein Structure, Tertiary | Bacteria - metabolism | Protein Structure, Secondary | Detergents - chemistry | Nanotechnology - methods | Streptomyces lividans - metabolism | Bacterial Proteins - chemistry | Phosphatidylcholines - chemistry | Lipids - chemistry | Phosphatidylglycerols - chemistry | Membrane Proteins - chemistry | Sodium Dodecyl Sulfate - chemistry | Bacteriorhodopsins - metabolism | Nanostructures - chemistry | Potassium Channels - chemistry | Cell Membrane - metabolism | Membrane Proteins - metabolism | Proteins - chemistry | Dimerization | Dimyristoylphosphatidylcholine - chemistry | Bacteriorhodopsin | Lipids | Rhodopsin | Surface active agents | Sulfates | Aquaporins
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5. Full Text Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs
by Bersch, Beate and Dörr, Jonas M and Hessel, Auey and Killian, J Antoinette and Schanda, Paul
Angewandte Chemie-International Edition, ISSN 1433-7851, 02/2017, Volume 56, Issue 9, pp. 2508–2512 - 2512
The structure, dynamics, and function of membrane proteins are intimately linked to the properties of the membrane environment in which the proteins are... 
coplymers | nanodiscs | membrane proteins | solid-state NMR | NMR spectroscopy | PHOSPHOLIPID-BILAYER NANODISCS | LIPODISQ | MALEIC ACID COPOLYMER | COMPLEXES | MICROSCOPY | CHEMISTRY, MULTIDISCIPLINARY | TRANSPORTER YIIP | NANOPARTICLES | PURIFICATION | MEMBRANE-PROTEINS | RECONSTITUTION | Protons | Bacterial Proteins - chemistry | Nanostructures - chemistry | Maleates - chemistry | Cupriavidus - chemistry | Diffusion | Zinc - chemistry | Proton Magnetic Resonance Spectroscopy - methods | Polystyrenes - chemistry | Membrane Transport Proteins - chemistry | Proteolipids - chemistry | Nuclear magnetic resonance spectroscopy | Aquaporins | Zinc | Structural integrity | Membranes | Nuclear magnetic resonance--NMR | Mimicry | Membrane proteins | Proteins | Magnetic resonance spectroscopy | Solid state | Spectrum analysis | Styrene | Maleic acid | Bacteria | Embedded structures | Structural analysis | Structure-function relationships | Index Medicus | Life Sciences | Biomolecules | Biochemistry, Molecular Biology | Chemical Sciences | membrane protein | styrene maleic acid
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6. 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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7. 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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8. Full Text Highly Permeable Polymeric Membranes Based on the Incorporation of the Functional Water Channel Protein Aquaporin Z
by Manish Kumar and Mariusz Grzelakowski and Julie Zilles and Mark Clark and Wolfgang Meier
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2007, Volume 104, Issue 52, pp. 20719 - 20724
The permeability and solute transport characteristics of amphiphilic triblock-polymer vesicles containing the bacterial water-channel protein Aquaporin Z... 
Water treatment | Copolymers | Light scattering | Aquaporins | Solutes | Cell membranes | Polymers | Activation energy | Block copolymers | P branes | Triblock copolymer | Permeability | water treatment | CHIP | TEMPERATURE | VESICLES | triblock copolymer | MULTIDISCIPLINARY SCIENCES | permeability | PROGRESS | FLUX | DESALINATION | TRIBLOCK COPOLYMER MEMBRANES | RECONSTITUTION | Temperature | Aquaporins - chemistry | Microscopy, Video | Water Purification | Drug Delivery Systems | Lipids - chemistry | Membrane Proteins - chemistry | Biochemistry - methods | Escherichia coli - metabolism | Water - chemistry | Membranes - chemistry | Polymers - chemistry | Protein Conformation | Kinetics | Escherichia coli Proteins - chemistry | Water | Evaluation | Purification | Chemical research | Properties | Methods | Proteins | Membranes | Solute movement | Index Medicus | Physical Sciences
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9. Full Text Chemistry and fabrication of polymeric nanofiltration membranes: A review
by Paul, Mou and Jons, Steven D
Polymer, ISSN 0032-3861, 10/2016, Volume 103, pp. 417 - 456
The review article describes research on different methods for manufacturing polymeric NF membranes. The primary focus is on NF composite membranes formed by... 
MPD | Fouling | Flux | Polymer | Salt rejection | Salt passage | Review | TMC | Nanofiltration | Amine | MgSO4 | PIP | Interfacial polymerization | NaCl | Membrane | Reverse osmosis | Coating | Water purification | Acid chloride | MgSO | IMPROVED WATER FLUX | POLY(ETHER ETHER KETONE) | LAYER-BY-LAYER | HOLLOW-FIBER MEMBRANES | TRIMETHYLALLYL AMMONIUM-CHLORIDE | POLYMER SCIENCE | REVERSE-OSMOSIS MEMBRANES | THIN-FILM-COMPOSITE | ORGANIC-SOLVENT NANOFILTRATION | LINKED POLYBENZIMIDAZOLE MEMBRANES | LOW-PRESSURE WATER | Chemical industry | Herbicides | Pesticides industry | Aquaporins | Polymerization | Porosity | Polymers | Rejection | Solvents | Membranes | Phase shift | Coatings
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