Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2015, Volume 112, Issue 3, pp. E259 - E266
The kinetics of folding–unfolding of a structurally diverse set of four proteins optimized for thermodynamic stability by rational redesign of surface...
Protein stability | Energy landscape | Charge-charge interaction | Protein folding | Computational design | energy landscape | charge–charge interaction | computational design | protein folding | protein stability | ELECTROSTATIC INTERACTIONS | PATHWAYS | III DOMAIN | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | NONNATIVE INTERACTIONS | charge-charge interaction | TOPOLOGICAL FRUSTRATION | SURFACE | MONTE-CARLO SIMULATION | SALT BRIDGES | Kinetics | Static Electricity | Computer Simulation | Protein Folding | Observations | Biological Sciences | PNAS Plus
Protein stability | Energy landscape | Charge-charge interaction | Protein folding | Computational design | energy landscape | charge–charge interaction | computational design | protein folding | protein stability | ELECTROSTATIC INTERACTIONS | PATHWAYS | III DOMAIN | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | NONNATIVE INTERACTIONS | charge-charge interaction | TOPOLOGICAL FRUSTRATION | SURFACE | MONTE-CARLO SIMULATION | SALT BRIDGES | Kinetics | Static Electricity | Computer Simulation | Protein Folding | Observations | Biological Sciences | PNAS Plus
Journal Article
2013, ISBN 9814355429, xvi, 257
Book
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2009, Volume 106, Issue 8, pp. 2601 - 2606
Here, we report the application of a computational approach that allows the rational design of enzymes with enhanced thermostability while retaining full...
Proteins | Aggregation | Enzymes | Protein engineering | Enzyme stability | Plasma stability | Protein stability | Amino acids | Biochemistry | Electrostatics | Computational design | ELECTROSTATIC INTERACTIONS | ACYLPHOSPHATASE | DESIGN | MECHANISM | UBIQUITIN | THERMOSTABILIZATION | MULTIDISCIPLINARY SCIENCES | protein stability | CDC42 | protein engineering | ACYL PHOSPHATASE | computational design | OPTIMIZATION | Enzymes - chemistry | Protein Conformation | Humans | Surface Properties | Protein Engineering | Thermal properties | Usage | Research | Structure | Methods | Computational biology | Biological Sciences
Proteins | Aggregation | Enzymes | Protein engineering | Enzyme stability | Plasma stability | Protein stability | Amino acids | Biochemistry | Electrostatics | Computational design | ELECTROSTATIC INTERACTIONS | ACYLPHOSPHATASE | DESIGN | MECHANISM | UBIQUITIN | THERMOSTABILIZATION | MULTIDISCIPLINARY SCIENCES | protein stability | CDC42 | protein engineering | ACYL PHOSPHATASE | computational design | OPTIMIZATION | Enzymes - chemistry | Protein Conformation | Humans | Surface Properties | Protein Engineering | Thermal properties | Usage | Research | Structure | Methods | Computational biology | Biological Sciences
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 05/2006, Volume 45, Issue 19, pp. 3022 - 3060
Almost all proteins contain charged amino acids. While the function in catalysis or binding of individual charges in the active site can often be identified,...
charge networks | charge regulation | proteins | capillary electrophoresis | electrostatic interactions | Proteins | Electrostatic interactions | Charge networks | Capillary electrophoresis | Charge regulation | 2ND VIRIAL-COEFFICIENTS | BARRIER HYDROGEN-BONDS | DEBYE-HUCKEL THEORY | ION TITRATION CURVE | BOVINE CARBONIC-ANHYDRASE | CHEMISTRY, MULTIDISCIPLINARY | COLD SHOCK PROTEIN | TRANSFER-RNA SYNTHETASE | IONIZATION MASS-SPECTROMETRY | POISSON-BOLTZMANN EQUATION | BETA-SHEET PROTEINS | Salts - chemistry | Thermodynamics | Molecular Probe Techniques | Amino Acids - chemistry | Ligands | Protein Conformation | Proteins - chemistry | Electrophoresis, Capillary - methods | Static Electricity | Binding Sites | Protein Folding
charge networks | charge regulation | proteins | capillary electrophoresis | electrostatic interactions | Proteins | Electrostatic interactions | Charge networks | Capillary electrophoresis | Charge regulation | 2ND VIRIAL-COEFFICIENTS | BARRIER HYDROGEN-BONDS | DEBYE-HUCKEL THEORY | ION TITRATION CURVE | BOVINE CARBONIC-ANHYDRASE | CHEMISTRY, MULTIDISCIPLINARY | COLD SHOCK PROTEIN | TRANSFER-RNA SYNTHETASE | IONIZATION MASS-SPECTROMETRY | POISSON-BOLTZMANN EQUATION | BETA-SHEET PROTEINS | Salts - chemistry | Thermodynamics | Molecular Probe Techniques | Amino Acids - chemistry | Ligands | Protein Conformation | Proteins - chemistry | Electrophoresis, Capillary - methods | Static Electricity | Binding Sites | Protein Folding
Journal Article
1976, ISBN 9780854321599, 25
Book
Journal of Computational Chemistry, ISSN 0192-8651, 01/2018, Volume 39, Issue 2, pp. 105 - 116
A low‐computational‐cost algorithm and its parallel implementation for periodic divide‐and‐conquer density‐functional tight‐binding (DC‐DFTB) calculations are...
density‐functional tight‐binding method | divide‐and‐conquer method | multipole expansion | periodic boundary condition | massively parallel calculation | density-functional tight-binding method | divide-and-conquer method | ELECTROSTATIC INTERACTIONS | WATER-SYSTEM | AB-INITIO | OPEN-SHELL SYSTEMS | PARTICLE MESH EWALD | FAST MULTIPOLE METHOD | ELECTRONIC-STRUCTURE CALCULATIONS | FRAGMENTATION METHODS | CHEMISTRY, MULTIDISCIPLINARY | SCC-DFTB | MOLECULAR-DYNAMICS SIMULATIONS | Multiprocessing | Specific gravity | Algorithms
density‐functional tight‐binding method | divide‐and‐conquer method | multipole expansion | periodic boundary condition | massively parallel calculation | density-functional tight-binding method | divide-and-conquer method | ELECTROSTATIC INTERACTIONS | WATER-SYSTEM | AB-INITIO | OPEN-SHELL SYSTEMS | PARTICLE MESH EWALD | FAST MULTIPOLE METHOD | ELECTRONIC-STRUCTURE CALCULATIONS | FRAGMENTATION METHODS | CHEMISTRY, MULTIDISCIPLINARY | SCC-DFTB | MOLECULAR-DYNAMICS SIMULATIONS | Multiprocessing | Specific gravity | Algorithms
Journal Article
Food Hydrocolloids, ISSN 0268-005X, 2009, Volume 23, Issue 3, pp. 765 - 772
The complex formation between β-lactoglobulin (β-lg) and pectin is studied using pectins with different physicochemical characteristics. Pectin allows for the...
Electrostatic interactions | Pectin | State diagrams | β-Lactoglobulin | Polysaccharide–protein complexes | Charge regulation | POLYELECTROLYTES | CARRAGEENAN | ACID | STABILIZATION | CONFORMATION | beta-Lactoglobulin | WHEY PROTEINS | AQUEOUS-SOLUTION | DEPENDENCE | Polysaccharide-protein complexes | COACERVATION | BOVINE SERUM-ALBUMIN | FOOD SCIENCE & TECHNOLOGY | CHEMISTRY, APPLIED | Charge density | Complex formation | Charge | pH | Mathematical models | Foods | Strength | acid | whey proteins | stabilization | aqueous-solution | carrageenan | coacervation | dependence | bovine serum-albumin | conformation | polyelectrolytes
Electrostatic interactions | Pectin | State diagrams | β-Lactoglobulin | Polysaccharide–protein complexes | Charge regulation | POLYELECTROLYTES | CARRAGEENAN | ACID | STABILIZATION | CONFORMATION | beta-Lactoglobulin | WHEY PROTEINS | AQUEOUS-SOLUTION | DEPENDENCE | Polysaccharide-protein complexes | COACERVATION | BOVINE SERUM-ALBUMIN | FOOD SCIENCE & TECHNOLOGY | CHEMISTRY, APPLIED | Charge density | Complex formation | Charge | pH | Mathematical models | Foods | Strength | acid | whey proteins | stabilization | aqueous-solution | carrageenan | coacervation | dependence | bovine serum-albumin | conformation | polyelectrolytes
Journal Article
Studies in electrical and electronic engineering, Volume 2, x, 441
Book
Angewandte Chemie International Edition, ISSN 1433-7851, 08/2016, Volume 55, Issue 33, pp. 9680 - 9684
Since the first prediction by Frenkel, many follow‐up studies have been carried out to show the presence of subsurface space‐charge layers having the opposite...
electron microscopy | surface chemistry | segregation | perovskite phases | electrostatic interactions | GRAIN-BOUNDARIES | IONIC-CRYSTALS | DEFECTS | SILVER-HALIDES | IMPURITIES | CHEMISTRY, MULTIDISCIPLINARY | ATOMS | EXCHANGE | LAYER | Perovskite | Ionic crystals | Consumer credit | Delinquency | Dopants | Surface charge | Scale (corrosion) | Solutes | Crystals
electron microscopy | surface chemistry | segregation | perovskite phases | electrostatic interactions | GRAIN-BOUNDARIES | IONIC-CRYSTALS | DEFECTS | SILVER-HALIDES | IMPURITIES | CHEMISTRY, MULTIDISCIPLINARY | ATOMS | EXCHANGE | LAYER | Perovskite | Ionic crystals | Consumer credit | Delinquency | Dopants | Surface charge | Scale (corrosion) | Solutes | Crystals
Journal Article
The Journal of Physical Chemistry B, ISSN 1520-6106, 10/2015, Volume 119, Issue 41, pp. 13103 - 13112
Charge–charge interactions play an important role in thermal stability of proteins. We employed an all-atom, native-topology-based model with non-native...
ELECTROSTATIC INTERACTIONS | FRUSTRATION | MOLECULAR-DYNAMICS | FUNNELS | III DOMAIN | DENATURED STATE ENSEMBLE | UNFOLDED STATE | CHEMISTRY, PHYSICAL | HUMAN TENASCIN | TRANSITION-STATE | ENERGY LANDSCAPE | Models, Molecular | Protein Stability | Proteins - chemistry | Static Electricity | Protein Folding | Molecular dynamics | Research | Protein folding | Analysis | Proteins | Residues | Stability | Dynamics | Fibronectin | Frustration | Folding | Thermal stability
ELECTROSTATIC INTERACTIONS | FRUSTRATION | MOLECULAR-DYNAMICS | FUNNELS | III DOMAIN | DENATURED STATE ENSEMBLE | UNFOLDED STATE | CHEMISTRY, PHYSICAL | HUMAN TENASCIN | TRANSITION-STATE | ENERGY LANDSCAPE | Models, Molecular | Protein Stability | Proteins - chemistry | Static Electricity | Protein Folding | Molecular dynamics | Research | Protein folding | Analysis | Proteins | Residues | Stability | Dynamics | Fibronectin | Frustration | Folding | Thermal stability
Journal Article
1971, NASA SP, Volume 276, viii, 34
Book
12.
Full Text
Collective bulk carrier delocalization driven by electrostatic surface charge accumulation
Nature, ISSN 0028-0836, 07/2012, Volume 487, Issue 7408, pp. 459 - 462
In the classic transistor, the number of electric charge carriers-and thus the electrical conductivity-is precisely controlled by external voltage, providing...
ELECTRIC-FIELD CONTROL | ROOM-TEMPERATURE | METAL-INSULATOR-TRANSITION | SUPERCONDUCTIVITY | EFFECT TRANSISTOR | MULTIDISCIPLINARY SCIENCES | MOTT TRANSITION | PHASE-TRANSITION | VO2 | VANADIUM DIOXIDE | BAND THEORY | Electric charge and distribution | Research | Transistors | Electrostatics | Electric properties | Temperature | Behavior | Semiconductors | Electric fields | Phase transitions | Carriers | Electric potential | Semiconductor devices | Metal-insulator transition | Voltage | Switching | Three dimensional
ELECTRIC-FIELD CONTROL | ROOM-TEMPERATURE | METAL-INSULATOR-TRANSITION | SUPERCONDUCTIVITY | EFFECT TRANSISTOR | MULTIDISCIPLINARY SCIENCES | MOTT TRANSITION | PHASE-TRANSITION | VO2 | VANADIUM DIOXIDE | BAND THEORY | Electric charge and distribution | Research | Transistors | Electrostatics | Electric properties | Temperature | Behavior | Semiconductors | Electric fields | Phase transitions | Carriers | Electric potential | Semiconductor devices | Metal-insulator transition | Voltage | Switching | Three dimensional
Journal Article
Langmuir, ISSN 0743-7463, 12/2018, Volume 34, Issue 51, pp. 15727 - 15738
The mechanisms of electrostatically driven adsorption of proteins on charged surfaces are studied with a new theoretical framework. The acid–base behavior,...
THIN-FILMS | CHYMOTRYPSIN | SPHERICAL POLYELECTROLYTE BRUSHES | MATERIALS SCIENCE, MULTIDISCIPLINARY | CHEMISTRY, PHYSICAL | SIMULATION | BETA-LACTOGLOBULIN | CHEMISTRY, MULTIDISCIPLINARY | HYDROGEN-ION EQUILIBRIA | LYSOZYME ADSORPTION | SURFACES | PREDICTION
THIN-FILMS | CHYMOTRYPSIN | SPHERICAL POLYELECTROLYTE BRUSHES | MATERIALS SCIENCE, MULTIDISCIPLINARY | CHEMISTRY, PHYSICAL | SIMULATION | BETA-LACTOGLOBULIN | CHEMISTRY, MULTIDISCIPLINARY | HYDROGEN-ION EQUILIBRIA | LYSOZYME ADSORPTION | SURFACES | PREDICTION
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 07/2016, Volume 55, Issue 30, pp. 8610 - 8614
Nanoparticles covered with ligand shells comprising both positively and negatively charged ligands exhibit Gram‐selective antibacterial action controlled by a...
ligands | surface charge | nanoparticles | Gram specificity | antibiotics | POLYMERS | ELECTROSTATIC TITRATIONS | STABILITY | ANTIBACTERIAL | ANTIMICROBIAL PEPTIDES | CHEMISTRY, MULTIDISCIPLINARY | STRATEGIES | POSITIVE BACTERIA | PROTEINS | RATIONAL DESIGN | Nanoparticles | Cells | Ligands | Index Medicus | catalysis (homogeneous), solar (photovoltaic), bio-inspired, charge transport, mesostructured materials, materials and chemistry by design, synthesis (novel materials), synthesis (self-assembly)
ligands | surface charge | nanoparticles | Gram specificity | antibiotics | POLYMERS | ELECTROSTATIC TITRATIONS | STABILITY | ANTIBACTERIAL | ANTIMICROBIAL PEPTIDES | CHEMISTRY, MULTIDISCIPLINARY | STRATEGIES | POSITIVE BACTERIA | PROTEINS | RATIONAL DESIGN | Nanoparticles | Cells | Ligands | Index Medicus | catalysis (homogeneous), solar (photovoltaic), bio-inspired, charge transport, mesostructured materials, materials and chemistry by design, synthesis (novel materials), synthesis (self-assembly)
Journal Article