The Plant Cell, ISSN 1040-4651, 11/2007, Volume 19, Issue 11, pp. 3403 - 3417
Many previous studies have provided evidence for genome changes in polyploids, but there are little data on the overall population dynamics of genome change...
Allopolyploidy | Polyploidy | Complementary DNA | Genetic variation | DNA | Linkage groups | Genomics | Genomes | Data lines | Methylation | ARABIDOPSIS POLYPLOIDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALLOPOLYPLOIDS | REARRANGEMENTS | CONCERTED EVOLUTION | PLANT SCIENCES | CELL BIOLOGY | QUANTITATIVE TRAIT LOCI | HOMEOLOGOUS RECOMBINATION | FLOWERING PLANTS | OILSEED RAPE | NICOTIANA | CYTOSINE METHYLATION | Chromosome Segregation | Brassica napus - genetics | Genome, Plant - genetics | RNA, Messenger - genetics | Genetic Markers | Phylogeny | Chromosomes, Plant - metabolism | DNA, Plant - metabolism | RNA, Messenger - metabolism | DNA Transposable Elements | Polymorphism, Single-Stranded Conformational | DNA Methylation | Phenotype | Gene Expression Regulation, Plant | Recombination, Genetic - genetics | DNA, Complementary - metabolism | Amplified Fragment Length Polymorphism Analysis | Genetic Linkage | Evaluation | Brassica | Gene mutations | Genetic aspects | Gene expression | Observations
Allopolyploidy | Polyploidy | Complementary DNA | Genetic variation | DNA | Linkage groups | Genomics | Genomes | Data lines | Methylation | ARABIDOPSIS POLYPLOIDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALLOPOLYPLOIDS | REARRANGEMENTS | CONCERTED EVOLUTION | PLANT SCIENCES | CELL BIOLOGY | QUANTITATIVE TRAIT LOCI | HOMEOLOGOUS RECOMBINATION | FLOWERING PLANTS | OILSEED RAPE | NICOTIANA | CYTOSINE METHYLATION | Chromosome Segregation | Brassica napus - genetics | Genome, Plant - genetics | RNA, Messenger - genetics | Genetic Markers | Phylogeny | Chromosomes, Plant - metabolism | DNA, Plant - metabolism | RNA, Messenger - metabolism | DNA Transposable Elements | Polymorphism, Single-Stranded Conformational | DNA Methylation | Phenotype | Gene Expression Regulation, Plant | Recombination, Genetic - genetics | DNA, Complementary - metabolism | Amplified Fragment Length Polymorphism Analysis | Genetic Linkage | Evaluation | Brassica | Gene mutations | Genetic aspects | Gene expression | Observations
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2005, Volume 127, Issue 22, pp. 8168 - 8173
Protein adhesion plays a major role in determining the biocompatibility of materials. The first stage of implant integration is the adhesion of protein...
ADHESION | HUMAN-SERUM-ALBUMIN | SPECTROSCOPY | BIOMATERIAL SURFACES | QUARTZ-CRYSTAL MICROBALANCE | SCANNING FORCE MICROSCOPY | INDUCED STRUCTURAL-CHANGES | BINDING | CHEMISTRY, MULTIDISCIPLINARY | FIBRINOGEN | POLYURETHANES | Gold - chemistry | Alcohols - chemistry | Coated Materials, Biocompatible - chemistry | Fibrinogen - chemistry | Spectroscopy, Fourier Transform Infrared | Wettability | Animals | Adsorption | Cattle | Surface Properties | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Serum Albumin, Bovine - chemistry | Sulfhydryl Compounds - chemistry | Alkanes - chemistry | Infrared spectroscopy | Protein research | Research | Analysis | Surface chemistry | Conformational analysis
ADHESION | HUMAN-SERUM-ALBUMIN | SPECTROSCOPY | BIOMATERIAL SURFACES | QUARTZ-CRYSTAL MICROBALANCE | SCANNING FORCE MICROSCOPY | INDUCED STRUCTURAL-CHANGES | BINDING | CHEMISTRY, MULTIDISCIPLINARY | FIBRINOGEN | POLYURETHANES | Gold - chemistry | Alcohols - chemistry | Coated Materials, Biocompatible - chemistry | Fibrinogen - chemistry | Spectroscopy, Fourier Transform Infrared | Wettability | Animals | Adsorption | Cattle | Surface Properties | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Serum Albumin, Bovine - chemistry | Sulfhydryl Compounds - chemistry | Alkanes - chemistry | Infrared spectroscopy | Protein research | Research | Analysis | Surface chemistry | Conformational analysis
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 45, pp. 18392 - 18407
p97 is an essential ATPase associated with various cellular activities (AAA(+)) that functions as a segregase in diverse cellular processes, including the...
VCP | VALOSIN-CONTAINING PROTEIN | POLYGLUTAMINE DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | cofactor binding | multisystem proteinopathy 1 (MSP1) | VCP/P97 | surface plasmon resonance (SPR) | ATPases associated with diverse cellular activities (AAA) | ENDOPLASMIC-RETICULUM STRESS | conformational change | proteostasis | PAGET-DISEASE | electron microscopy (EM) | p97 | UBIQUITIN CHAINS | STRUCTURAL BASIS | MACHADO-JOSEPH-DISEASE | MOUSE MODEL | ataxin3 | nucleotide regulation | CRYO-EM STRUCTURE | Proteostasis Deficiencies - metabolism | Coenzymes - genetics | Humans | Protein Multimerization | Crystallography, X-Ray | Adenosine Diphosphate - chemistry | Recombinant Fusion Proteins - metabolism | Coenzymes - metabolism | Adenosine Triphosphate - metabolism | Databases, Protein | Distal Myopathies - metabolism | Proteostasis Deficiencies - enzymology | Ataxin-3 - chemistry | Protein Interaction Domains and Motifs | Valosin Containing Protein - chemistry | Ataxin-3 - metabolism | Coenzymes - chemistry | Binding Sites | Peptide Fragments - genetics | Repressor Proteins - metabolism | Binding, Competitive | Microscopy, Electron, Transmission | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Valosin Containing Protein - genetics | Valosin Containing Protein - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Protein Interaction Mapping | Distal Myopathies - enzymology | Proteostasis Deficiencies - genetics | Distal Myopathies - genetics | Peptide Fragments - chemistry | Protein Conformation | Adenosine Diphosphate - metabolism | Mutation | Adenosine Triphosphate - chemistry | Amino Acid Substitution | Ataxin-3 - genetics | Molecular Bases of Disease
VCP | VALOSIN-CONTAINING PROTEIN | POLYGLUTAMINE DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | cofactor binding | multisystem proteinopathy 1 (MSP1) | VCP/P97 | surface plasmon resonance (SPR) | ATPases associated with diverse cellular activities (AAA) | ENDOPLASMIC-RETICULUM STRESS | conformational change | proteostasis | PAGET-DISEASE | electron microscopy (EM) | p97 | UBIQUITIN CHAINS | STRUCTURAL BASIS | MACHADO-JOSEPH-DISEASE | MOUSE MODEL | ataxin3 | nucleotide regulation | CRYO-EM STRUCTURE | Proteostasis Deficiencies - metabolism | Coenzymes - genetics | Humans | Protein Multimerization | Crystallography, X-Ray | Adenosine Diphosphate - chemistry | Recombinant Fusion Proteins - metabolism | Coenzymes - metabolism | Adenosine Triphosphate - metabolism | Databases, Protein | Distal Myopathies - metabolism | Proteostasis Deficiencies - enzymology | Ataxin-3 - chemistry | Protein Interaction Domains and Motifs | Valosin Containing Protein - chemistry | Ataxin-3 - metabolism | Coenzymes - chemistry | Binding Sites | Peptide Fragments - genetics | Repressor Proteins - metabolism | Binding, Competitive | Microscopy, Electron, Transmission | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Valosin Containing Protein - genetics | Valosin Containing Protein - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Protein Interaction Mapping | Distal Myopathies - enzymology | Proteostasis Deficiencies - genetics | Distal Myopathies - genetics | Peptide Fragments - chemistry | Protein Conformation | Adenosine Diphosphate - metabolism | Mutation | Adenosine Triphosphate - chemistry | Amino Acid Substitution | Ataxin-3 - genetics | Molecular Bases of Disease
Journal Article
BBA - Biomembranes, ISSN 0005-2736, 10/2015, Volume 1848, Issue 10, pp. 2065 - 2074
EmrE protein transports positively charged aromatic drugs (xenobiotics) in exchange for two protons and thus provides bacteria resistance to variety of drugs....
Molecular dynamics | Small multidrug resistance (SMR) transporter | EmrE | Multidrug transporter | Heterogeneous lipid bilayer | DOMAIN | RECOGNITION | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BILAYERS | CONFORMATIONAL-CHANGES | BIOPHYSICS | LANGEVIN | RESISTANCE | PROVIDES | BINDING | PLASTICITY | Hydrogen | Analysis | Chemical properties
Molecular dynamics | Small multidrug resistance (SMR) transporter | EmrE | Multidrug transporter | Heterogeneous lipid bilayer | DOMAIN | RECOGNITION | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BILAYERS | CONFORMATIONAL-CHANGES | BIOPHYSICS | LANGEVIN | RESISTANCE | PROVIDES | BINDING | PLASTICITY | Hydrogen | Analysis | Chemical properties
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2015, Volume 112, Issue 24, pp. 1 - 6
Research on change-point detection, the classical problem of detecting abrupt changes in sequential data, has focused predominantly on datasets with a single...
Penalized maximum likelihood | Molecular dynamics | SIMPLE | Conformational change | Multivariate | multivariate | penalized maximum likelihood | conformational change | molecular dynamics | SEQUENCES | MODELS | MULTIDISCIPLINARY SCIENCES | MOLECULAR-DYNAMICS TRAJECTORIES | VARIABLES | PROTEINS | DISCOVERY | Likelihood Functions | Algorithms | Biophysical Phenomena | Protein Conformation | Molecular Dynamics Simulation - statistics & numerical data | Proteins - chemistry | Protein Folding | Electronic data processing | Usage | Statistical methods | Methods | Biological Sciences | Physical Sciences
Penalized maximum likelihood | Molecular dynamics | SIMPLE | Conformational change | Multivariate | multivariate | penalized maximum likelihood | conformational change | molecular dynamics | SEQUENCES | MODELS | MULTIDISCIPLINARY SCIENCES | MOLECULAR-DYNAMICS TRAJECTORIES | VARIABLES | PROTEINS | DISCOVERY | Likelihood Functions | Algorithms | Biophysical Phenomena | Protein Conformation | Molecular Dynamics Simulation - statistics & numerical data | Proteins - chemistry | Protein Folding | Electronic data processing | Usage | Statistical methods | Methods | Biological Sciences | Physical Sciences
Journal Article
Electrochemistry Communications, ISSN 1388-2481, 02/2013, Volume 27, pp. 104 - 107
Chronopotentiometric stripping (CPS) analysis was used to show that transmembrane protein Na /K -ATPase (NKA) structural changes can be observed in the...
Sodium–potassium pump | Structural changes | Chronopotentiometry | Electroanalysis | Membrane protein | Mercury electrode | Sodium-potassium pump | STRIPPING CHRONOPOTENTIOMETRY | ELECTROCHEMISTRY | METALLOTHIONEIN | CRYSTAL-STRUCTURE | HYDROGEN EVOLUTION | MERCURY-ELECTRODES | CARBON ELECTRODES | CONFORMATIONAL-CHANGES | CYTOPLASMIC HEADPIECE | CALCIUM-PUMP | BOVINE SERUM-ALBUMIN
Sodium–potassium pump | Structural changes | Chronopotentiometry | Electroanalysis | Membrane protein | Mercury electrode | Sodium-potassium pump | STRIPPING CHRONOPOTENTIOMETRY | ELECTROCHEMISTRY | METALLOTHIONEIN | CRYSTAL-STRUCTURE | HYDROGEN EVOLUTION | MERCURY-ELECTRODES | CARBON ELECTRODES | CONFORMATIONAL-CHANGES | CYTOPLASMIC HEADPIECE | CALCIUM-PUMP | BOVINE SERUM-ALBUMIN
Journal Article
Nature, ISSN 0028-0836, 12/2010, Volume 468, Issue 7324, pp. 705 - 708
Alphaviruses are enveloped RNA viruses that have a diameter of about 700 Å and can be lethal human pathogens. Entry of virus into host cells by endocytosis is...
MEMBRANE-FUSION | PH-DEPENDENT FUSION | SINDBIS VIRUS | DYNAMIC ENVELOPE | CONFORMATIONAL-CHANGE | PRECURSOR | MULTIDISCIPLINARY SCIENCES | SEMLIKI-FOREST-VIRUS | GLYCOPROTEIN | CLASS-II VIRUS | Viral Fusion Proteins - metabolism | Membrane Glycoproteins - metabolism | Receptors, Virus - metabolism | Membrane Glycoproteins - chemistry | Protein Multimerization | Crystallography, X-Ray | Virion - chemistry | Endosomes - metabolism | Virus Internalization | Sindbis Virus - metabolism | Sindbis Virus - chemistry | Viral Fusion Proteins - chemistry | Protein Structure, Quaternary | Viral Envelope Proteins - metabolism | Protein Structure, Tertiary | Cell Line | Membrane Fusion | Models, Molecular | Virion - metabolism | Cryoelectron Microscopy | Animals | Viral Envelope Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Drosophila melanogaster | Hydrogen-Ion Concentration | RNA viruses | Physiological aspects | Glycoproteins | Research | Structure | Health aspects | Protein binding | Pathology | Virology | Crystal structure
MEMBRANE-FUSION | PH-DEPENDENT FUSION | SINDBIS VIRUS | DYNAMIC ENVELOPE | CONFORMATIONAL-CHANGE | PRECURSOR | MULTIDISCIPLINARY SCIENCES | SEMLIKI-FOREST-VIRUS | GLYCOPROTEIN | CLASS-II VIRUS | Viral Fusion Proteins - metabolism | Membrane Glycoproteins - metabolism | Receptors, Virus - metabolism | Membrane Glycoproteins - chemistry | Protein Multimerization | Crystallography, X-Ray | Virion - chemistry | Endosomes - metabolism | Virus Internalization | Sindbis Virus - metabolism | Sindbis Virus - chemistry | Viral Fusion Proteins - chemistry | Protein Structure, Quaternary | Viral Envelope Proteins - metabolism | Protein Structure, Tertiary | Cell Line | Membrane Fusion | Models, Molecular | Virion - metabolism | Cryoelectron Microscopy | Animals | Viral Envelope Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Drosophila melanogaster | Hydrogen-Ion Concentration | RNA viruses | Physiological aspects | Glycoproteins | Research | Structure | Health aspects | Protein binding | Pathology | Virology | Crystal structure
Journal Article
Nature Biotechnology, ISSN 1087-0156, 10/2014, Volume 32, Issue 10, pp. 1036 - 1044
Changes in protein conformation can affect protein function, but methods to probe these structural changes on a global scale in cells have been lacking. To...
YEAST | LIMITED PROTEOLYSIS | CONFORMATIONAL-CHANGES | MOLTEN GLOBULE | PHOSPHORYLATION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SECONDARY STRUCTURE | SCALE | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | TARGETED PROTEOMICS | Fructosediphosphates | Amino Acid Sequence | Peptide Fragments | Molecular Sequence Data | Proteins - analysis | Proteome - analysis | Proteome - chemistry | Trypsin | Proteolysis | Mass Spectrometry | Prions | Protein Conformation | Amyloid | Proteins - chemistry | Proteomics - methods | Proteins | Protein research | Research | Structure | Conformation | Data analysis | Cells | Proteomics
YEAST | LIMITED PROTEOLYSIS | CONFORMATIONAL-CHANGES | MOLTEN GLOBULE | PHOSPHORYLATION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SECONDARY STRUCTURE | SCALE | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | TARGETED PROTEOMICS | Fructosediphosphates | Amino Acid Sequence | Peptide Fragments | Molecular Sequence Data | Proteins - analysis | Proteome - analysis | Proteome - chemistry | Trypsin | Proteolysis | Mass Spectrometry | Prions | Protein Conformation | Amyloid | Proteins - chemistry | Proteomics - methods | Proteins | Protein research | Research | Structure | Conformation | Data analysis | Cells | Proteomics
Journal Article
Biochemistry, ISSN 0006-2960, 09/2017, Volume 56, Issue 36, pp. 4808 - 4818
Amyloid formation of natively folded proteins involves global and/or local unfolding of the native state to form aggregation-prone intermediates. Here we...
SOLID-STATE NMR | WILD-TYPE TRANSTHYRETIN | SPECTROSCOPY | THERMODYNAMIC ANALYSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONFORMATIONAL FLEXIBILITY | INTERMEDIATE | MOLECULAR-DYNAMICS SIMULATIONS | MEMBRANE-PROTEINS | SUBUNIT INTERFACE | AMYLOID FIBRIL FORMATION | Gene Expression | Magnetic Resonance Spectroscopy | Oxidation-Reduction | Time Factors | Escherichia coli - metabolism | Models, Molecular | Protein Binding | Protein Conformation | Prealbumin - chemistry | Mutation | Circular Dichroism | Protein Folding | Chemical reactions | Nuclear magnetic resonance spectroscopy | Usage | Research | Gene mutations | PDSD | Solid-state NMR | TTR | amyloidosis | L55P | SPROX | mass spectrometry | Amyloid | V30M | misfolding
SOLID-STATE NMR | WILD-TYPE TRANSTHYRETIN | SPECTROSCOPY | THERMODYNAMIC ANALYSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONFORMATIONAL FLEXIBILITY | INTERMEDIATE | MOLECULAR-DYNAMICS SIMULATIONS | MEMBRANE-PROTEINS | SUBUNIT INTERFACE | AMYLOID FIBRIL FORMATION | Gene Expression | Magnetic Resonance Spectroscopy | Oxidation-Reduction | Time Factors | Escherichia coli - metabolism | Models, Molecular | Protein Binding | Protein Conformation | Prealbumin - chemistry | Mutation | Circular Dichroism | Protein Folding | Chemical reactions | Nuclear magnetic resonance spectroscopy | Usage | Research | Gene mutations | PDSD | Solid-state NMR | TTR | amyloidosis | L55P | SPROX | mass spectrometry | Amyloid | V30M | misfolding
Journal Article
Food Chemistry, ISSN 0308-8146, 02/2019, Volume 274, pp. 547 - 557
The aim of this study was to analyze the effect of AAPH on the conformational structure and allergenicity of shrimp tropomyosin (TM). The structure of AAPH-TM...
Shrimp tropomyosin | Protein oxidation | Allergenicity | AAPH | DL-lysine (PubChem CID: 866) | L-leucine (PubChem CID: 6106) | 1-Anilino-8-naphthalene-sulfonate (PubChem CID: 1369) | 3,3′,5,5′-Tetramethylbenzidine (PubChem CID: 41206) | Acrylamide (PubChem CID: 6579) | Brilliant Blue R (PubChem CID: 61365) | DL-Dithiothreitol (PubChem CID: 446094) | IGE BINDING-CAPACITY | HIGH-PRESSURE | FOOD SCIENCE & TECHNOLOGY | CROSS-LINKING | HEAT-TREATMENT | METAPENAEUS-ENSIS TROPOMYOSIN | NUTRITION & DIETETICS | CONFORMATIONAL STRUCTURE | EGG-WHITE | OXIDATIVE MODIFICATION | CHEMISTRY, APPLIED | SOY-PROTEIN | POTENTIAL ALLERGENICITY | Animals | Allergens - immunology | Tropomyosin - immunology | Allergens - chemistry | Mice | Penaeidae - chemistry | Tropomyosin - chemistry | Amidines - chemistry | Shellfish - analysis | Immunoglobulin E - chemistry | Penaeidae - immunology | Index Medicus
Shrimp tropomyosin | Protein oxidation | Allergenicity | AAPH | DL-lysine (PubChem CID: 866) | L-leucine (PubChem CID: 6106) | 1-Anilino-8-naphthalene-sulfonate (PubChem CID: 1369) | 3,3′,5,5′-Tetramethylbenzidine (PubChem CID: 41206) | Acrylamide (PubChem CID: 6579) | Brilliant Blue R (PubChem CID: 61365) | DL-Dithiothreitol (PubChem CID: 446094) | IGE BINDING-CAPACITY | HIGH-PRESSURE | FOOD SCIENCE & TECHNOLOGY | CROSS-LINKING | HEAT-TREATMENT | METAPENAEUS-ENSIS TROPOMYOSIN | NUTRITION & DIETETICS | CONFORMATIONAL STRUCTURE | EGG-WHITE | OXIDATIVE MODIFICATION | CHEMISTRY, APPLIED | SOY-PROTEIN | POTENTIAL ALLERGENICITY | Animals | Allergens - immunology | Tropomyosin - immunology | Allergens - chemistry | Mice | Penaeidae - chemistry | Tropomyosin - chemistry | Amidines - chemistry | Shellfish - analysis | Immunoglobulin E - chemistry | Penaeidae - immunology | Index Medicus
Journal Article
CHEMICAL COMMUNICATIONS, ISSN 1359-7345, 2016, Volume 52, Issue 79, pp. 11752 - 11755
A preferred-handed helicity induced in an optically-inactive poly(phenyleneethynylene)-based foldamer bearing carboxylic acid pendants upon complexation with a...
SENSE INVERSION | SCREW-SENSE | MAIN-CHAIN | CONFORMATIONAL-CHANGE | CIRCULAR-DICHROISM | PHENYLENE ETHYNYLENE OLIGOMERS | MACROMOLECULAR HELICITY | POLY(PHENYLACETYLENE)S BEARING | CHAIN-LENGTH DEPENDENCE | CHIRAL AMPLIFICATION | CHEMISTRY, MULTIDISCIPLINARY | Complexation | Diamines | Stability | Inversions | Helices | Carboxylic acids | Helicity | Bearing
SENSE INVERSION | SCREW-SENSE | MAIN-CHAIN | CONFORMATIONAL-CHANGE | CIRCULAR-DICHROISM | PHENYLENE ETHYNYLENE OLIGOMERS | MACROMOLECULAR HELICITY | POLY(PHENYLACETYLENE)S BEARING | CHAIN-LENGTH DEPENDENCE | CHIRAL AMPLIFICATION | CHEMISTRY, MULTIDISCIPLINARY | Complexation | Diamines | Stability | Inversions | Helices | Carboxylic acids | Helicity | Bearing
Journal Article
Quarterly Reviews of Biophysics, ISSN 0033-5835, 05/2013, Volume 46, Issue 2, pp. 181 - 209
Formation of protein-ligand complexes causes various changes in both the receptor and the ligand. This review focuses on changes in pK and protonation states...
ELECTROSTATIC INTERACTIONS | FREE-ENERGY CALCULATIONS | PK(A) VALUES | IONIZATION STATES | CONFORMATIONAL-CHANGES | BIOPHYSICS | HYDROGEN-BOND | CATALYTIC ASPARTYL GROUPS | PH MOLECULAR-DYNAMICS | HIV-1 PROTEASE | IONIZABLE GROUPS | Protons | Proteins - metabolism | Humans | Protein Binding | Ligands | Molecular Docking Simulation | Hydrogen-Ion Concentration | Proteins | Biophysics | Molecular biology | Binding sites | Drugs | Binding | Computation | Ionization | Binding energy | Protonation | Optimization
ELECTROSTATIC INTERACTIONS | FREE-ENERGY CALCULATIONS | PK(A) VALUES | IONIZATION STATES | CONFORMATIONAL-CHANGES | BIOPHYSICS | HYDROGEN-BOND | CATALYTIC ASPARTYL GROUPS | PH MOLECULAR-DYNAMICS | HIV-1 PROTEASE | IONIZABLE GROUPS | Protons | Proteins - metabolism | Humans | Protein Binding | Ligands | Molecular Docking Simulation | Hydrogen-Ion Concentration | Proteins | Biophysics | Molecular biology | Binding sites | Drugs | Binding | Computation | Ionization | Binding energy | Protonation | Optimization
Journal Article
British Journal of Pharmacology, ISSN 0007-1188, 03/2008, Volume 153, Issue S1, pp. S358 - S366
The G‐protein‐coupled receptors (GPCRs) represent one the largest families of drug targets. Upon agonist binding a receptor undergoes conformational...
G‐protein‐coupled receptors | conformational changes | FRET | 7‐TM | FlAsH‐EDT2 | functional selectivity | FlAsH-EDT | Conformational changes | 7-TM | Functional selectivity | G-protein-coupled receptors | BETA ADRENERGIC-RECEPTOR | TOGGLE SWITCH MODEL | RESONANCE ENERGY-TRANSFER | PARTIAL AGONISM | MUSCARINIC ACETYLCHOLINE-RECEPTOR | TRANSMEMBRANE DOMAINS III | GREEN FLUORESCENT PROTEIN | OPIOID RECEPTOR | PHARMACOLOGY & PHARMACY | FlAsH-EDT2 | DISULFIDE CROSS-LINKING | LIVING CELLS | Humans | Receptor, Muscarinic M3 - drug effects | Receptor, Muscarinic M3 - chemistry | Chelating Agents - pharmacology | Receptors, Adrenergic, beta-2 - drug effects | Receptors, Adrenergic, beta-2 - chemistry | Receptors, Drug - chemistry | Animals | Receptors, Drug - drug effects | Fluorescence Resonance Energy Transfer | Protein Conformation | Rhodopsin - drug effects | Receptors, G-Protein-Coupled - drug effects | Receptors, G-Protein-Coupled - chemistry | Rhodopsin - chemistry | Review
G‐protein‐coupled receptors | conformational changes | FRET | 7‐TM | FlAsH‐EDT2 | functional selectivity | FlAsH-EDT | Conformational changes | 7-TM | Functional selectivity | G-protein-coupled receptors | BETA ADRENERGIC-RECEPTOR | TOGGLE SWITCH MODEL | RESONANCE ENERGY-TRANSFER | PARTIAL AGONISM | MUSCARINIC ACETYLCHOLINE-RECEPTOR | TRANSMEMBRANE DOMAINS III | GREEN FLUORESCENT PROTEIN | OPIOID RECEPTOR | PHARMACOLOGY & PHARMACY | FlAsH-EDT2 | DISULFIDE CROSS-LINKING | LIVING CELLS | Humans | Receptor, Muscarinic M3 - drug effects | Receptor, Muscarinic M3 - chemistry | Chelating Agents - pharmacology | Receptors, Adrenergic, beta-2 - drug effects | Receptors, Adrenergic, beta-2 - chemistry | Receptors, Drug - chemistry | Animals | Receptors, Drug - drug effects | Fluorescence Resonance Energy Transfer | Protein Conformation | Rhodopsin - drug effects | Receptors, G-Protein-Coupled - drug effects | Receptors, G-Protein-Coupled - chemistry | Rhodopsin - chemistry | Review
Journal Article