Polyhedron, ISSN 0277-5387, 01/2019, Volume 158, pp. 36 - 46
Novel palladium(II) and platinum(II) complexes featuring amides of tetrazol-1-yl- and tetrazol-5-ylacetic acids were synthesized. The palladium(II) complexes...
Tetrazolylacetamides | Interaction with BSA/DNA | Palladium(II) and platinum(II) complexes | Molecular docking | Anti-cancer and antimicrobial activities | PROTEIN | TETRAZOLYLACETIC ACIDS | AGENTS | CRYSTALLOGRAPHY | CYTOTOXICITY | METAL-COMPLEXES | CHEMISTRY, INORGANIC & NUCLEAR
Tetrazolylacetamides | Interaction with BSA/DNA | Palladium(II) and platinum(II) complexes | Molecular docking | Anti-cancer and antimicrobial activities | PROTEIN | TETRAZOLYLACETIC ACIDS | AGENTS | CRYSTALLOGRAPHY | CYTOTOXICITY | METAL-COMPLEXES | CHEMISTRY, INORGANIC & NUCLEAR
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2014, Volume 9, Issue 7, p. e103878
Fluorescence is a proven tool in all fields of knowledge, including biology and medicine. A significant obstacle in its use is the nonlinearity of the...
AMYLOID FIBRILS | PHOTOLUMINESCENCE | LUMINESCENCE | QUANTUM YIELD | MULTIDISCIPLINARY SCIENCES | ABSORPTION | SPECTRA | EMISSION | RIGHT-ANGLE | BINDING | THIOFLAVIN T | Fluorescent Dyes - chemistry | Spectrometry, Fluorescence - methods | Quantum Theory | Spectrometry, Fluorescence - instrumentation | Filtration - instrumentation | Solutions - chemistry | Fluorescence | Dyes | Laboratories | Macromolecules | Fluorescent dyes | Reabsorption | Fluorescent indicators | Slits | Biophysics | Spectral analysis | Studies | Luminous intensity | Absorbance | Dilution | Cellular biology | Protein folding | Spectrum analysis | Absorption spectra | Energy transfer | Nonlinear systems | Methods
AMYLOID FIBRILS | PHOTOLUMINESCENCE | LUMINESCENCE | QUANTUM YIELD | MULTIDISCIPLINARY SCIENCES | ABSORPTION | SPECTRA | EMISSION | RIGHT-ANGLE | BINDING | THIOFLAVIN T | Fluorescent Dyes - chemistry | Spectrometry, Fluorescence - methods | Quantum Theory | Spectrometry, Fluorescence - instrumentation | Filtration - instrumentation | Solutions - chemistry | Fluorescence | Dyes | Laboratories | Macromolecules | Fluorescent dyes | Reabsorption | Fluorescent indicators | Slits | Biophysics | Spectral analysis | Studies | Luminous intensity | Absorbance | Dilution | Cellular biology | Protein folding | Spectrum analysis | Absorption spectra | Energy transfer | Nonlinear systems | Methods
Journal Article
Russian Journal of General Chemistry, ISSN 1070-3632, 11/2018, Volume 88, Issue 11, pp. 2354 - 2358
A series of trans-palladium(II) complexes (trans-[PdCl2L2], L = ethyl 5-R-2H-tetrazol-2-ylacetate, 5-R-2H-tetrazol-2-ylacetamides, R = Me, Ph) has been...
interaction with DNA | Chemistry | tetrazole-containing Pd(II) complexes | Chemistry/Food Science, general | tetrazol-2-ylacetic acid derivatives | antiproliferative activity | DNA | PLATINUM | AGENTS | FEATURING TETRAZOLYLACETIC ACIDS | BINDING | CHEMISTRY, MULTIDISCIPLINARY | METAL-COMPLEXES
interaction with DNA | Chemistry | tetrazole-containing Pd(II) complexes | Chemistry/Food Science, general | tetrazol-2-ylacetic acid derivatives | antiproliferative activity | DNA | PLATINUM | AGENTS | FEATURING TETRAZOLYLACETIC ACIDS | BINDING | CHEMISTRY, MULTIDISCIPLINARY | METAL-COMPLEXES
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 08/2019, Volume 44, Issue 8, pp. 716 - 728
At the turn of this century, cardinal changes took place in the perceptions of the structure and function of proteins, as well as in the organizational...
emergent behavior | edge of chaos | biological soft matter | liquid-liquid phase transition | CELLS | MOLECULAR RECOGNITION FEATURES | BIOCHEMISTRY & MOLECULAR BIOLOGY | REGIONS | FUZZY COMPLEXES | DYNAMICS | COUPLED RECEPTORS | LIQUID DROPLETS | TRANSITIONS | P GRANULES | BINDING | Proteins | Medical colleges | Analysis | Membranes | Phase separation | Biochemistry | Stochasticity | Organelles | Structure-function relationships
emergent behavior | edge of chaos | biological soft matter | liquid-liquid phase transition | CELLS | MOLECULAR RECOGNITION FEATURES | BIOCHEMISTRY & MOLECULAR BIOLOGY | REGIONS | FUZZY COMPLEXES | DYNAMICS | COUPLED RECEPTORS | LIQUID DROPLETS | TRANSITIONS | P GRANULES | BINDING | Proteins | Medical colleges | Analysis | Membranes | Phase separation | Biochemistry | Stochasticity | Organelles | Structure-function relationships
Journal Article
Cellular and Molecular Life Sciences, ISSN 1420-682X, 11/2018, Volume 75, Issue 21, pp. 3907 - 3929
Effects of macromolecular crowding on structural and functional properties of ordered proteins, their folding, interactability, and aggregation are well...
Life Sciences | Biomedicine, general | Biochemistry, general | Macromolecular crowding | Induced folding | Life Sciences, general | Proteinaceous membrane-less organelles | Conformational stability | Intrinsically disordered protein region | Intrinsically disordered protein | Cell Biology | SINGLE-MOLECULE SPECTROSCOPY | ANTI-SIGMA FACTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-SCATTERING | ALPHA-SYNUCLEIN | RIBONUCLEASE-P-PROTEIN | CELL BIOLOGY | NATIVELY UNFOLDED PROTEINS | PHASE-SEPARATION | C-TERMINAL DOMAIN | MEMBRANE-LESS ORGANELLES | ANGLE NEUTRON-SCATTERING | Proteins | Physiological aspects | Analysis | Macromolecules | Environment | Organelles | Phase transitions | Folding | Environmental effects | Crowding | Cellular structure | Structure-function relationships
Life Sciences | Biomedicine, general | Biochemistry, general | Macromolecular crowding | Induced folding | Life Sciences, general | Proteinaceous membrane-less organelles | Conformational stability | Intrinsically disordered protein region | Intrinsically disordered protein | Cell Biology | SINGLE-MOLECULE SPECTROSCOPY | ANTI-SIGMA FACTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-SCATTERING | ALPHA-SYNUCLEIN | RIBONUCLEASE-P-PROTEIN | CELL BIOLOGY | NATIVELY UNFOLDED PROTEINS | PHASE-SEPARATION | C-TERMINAL DOMAIN | MEMBRANE-LESS ORGANELLES | ANGLE NEUTRON-SCATTERING | Proteins | Physiological aspects | Analysis | Macromolecules | Environment | Organelles | Phase transitions | Folding | Environmental effects | Crowding | Cellular structure | Structure-function relationships
Journal Article
Journal of Molecular Structure, ISSN 0022-2860, 06/2015, Volume 1090, pp. 107 - 111
Spectral characteristics (absorption spectra, excitation and emission spectra of solvatochromic dye 6-bromo-acetyl-2-dimethylamino-naphtalene (BADAN) were...
Fluorescence | Excitation and emission spectra | Solvatochromism | BADAN | Inner-filter effect | Absorption spectra | EXCITED-STATE | GLUCOSE/GALACTOSE-BINDING PROTEIN | ENVIRONMENT | CHEMISTRY, PHYSICAL | PHOTOPHYSICAL PROPERTIES | FLUORESCENCE-SPECTRA | ABSORPTION | PRODAN POSSESS | DERIVATIVES | PROBE | DIPOLE-MOMENTS | Nitriles
Fluorescence | Excitation and emission spectra | Solvatochromism | BADAN | Inner-filter effect | Absorption spectra | EXCITED-STATE | GLUCOSE/GALACTOSE-BINDING PROTEIN | ENVIRONMENT | CHEMISTRY, PHYSICAL | PHOTOPHYSICAL PROPERTIES | FLUORESCENCE-SPECTRA | ABSORPTION | PRODAN POSSESS | DERIVATIVES | PROBE | DIPOLE-MOMENTS | Nitriles
Journal Article
Molecules, ISSN 1420-3049, 02/2017, Volume 22, Issue 2, pp. 244 - 244
Conformational changes of d-glucose/d-galactose-binding protein (GGBP) were studied under molecular crowding conditions modeled by concentrated solutions of...
Macromolecular crowding | Protein aggregation | Intrinsic fluorescence | Protein folding | Protein unfolding | D-glucose/D-galactose-binding protein | Polymers | Circular dichroism | d-galactose-binding protein | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | intrinsic fluorescence | circular dichroism | CHEMISTRY, MULTIDISCIPLINARY | SHAPE | protein unfolding | macromolecular crowding | protein aggregation | d-glucose | protein folding | polymers | CELL | AGGREGATION | Calcium-Binding Proteins - chemistry | Calcium-Binding Proteins - metabolism | Periplasmic Binding Proteins - chemistry | Protein Unfolding | Molecular Conformation | Protein Refolding | Models, Molecular | Structure-Activity Relationship | Glucose - chemistry | Glucose - metabolism | Monosaccharide Transport Proteins - chemistry | Monosaccharide Transport Proteins - metabolism | Periplasmic Binding Proteins - metabolism | Macromolecules | Guanidine | Fluorescence | Guanidines | Compaction | Glucose | Crowding | Dextran | Proteins | Polyethylene glycol | Guanidine hydrochloride | Galactose | Protein interaction | D-Galactose | Sugar | d-galactose-binding protein">">d-galactose-binding protein | d-glucose">">d-glucose
Macromolecular crowding | Protein aggregation | Intrinsic fluorescence | Protein folding | Protein unfolding | D-glucose/D-galactose-binding protein | Polymers | Circular dichroism | d-galactose-binding protein | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | intrinsic fluorescence | circular dichroism | CHEMISTRY, MULTIDISCIPLINARY | SHAPE | protein unfolding | macromolecular crowding | protein aggregation | d-glucose | protein folding | polymers | CELL | AGGREGATION | Calcium-Binding Proteins - chemistry | Calcium-Binding Proteins - metabolism | Periplasmic Binding Proteins - chemistry | Protein Unfolding | Molecular Conformation | Protein Refolding | Models, Molecular | Structure-Activity Relationship | Glucose - chemistry | Glucose - metabolism | Monosaccharide Transport Proteins - chemistry | Monosaccharide Transport Proteins - metabolism | Periplasmic Binding Proteins - metabolism | Macromolecules | Guanidine | Fluorescence | Guanidines | Compaction | Glucose | Crowding | Dextran | Proteins | Polyethylene glycol | Guanidine hydrochloride | Galactose | Protein interaction | D-Galactose | Sugar | d-galactose-binding protein">">d-galactose-binding protein | d-glucose">">d-glucose
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 09/2017, Volume 18, Issue 9, p. 2008
The ability of D-glucose/D-galactose-binding protein (GGBP) to reversibly interact with its ligands, glucose and galactose, makes this protein an attractive...
Fluorescent label BADAN | Conformational ensemble | Osmolyte-like stabilizing effect | Protein function | Guanidine hydrochloride | D-glucose/D-galactose-binding protein | Protein conformers | protein conformers | fluorescent label BADAN | conformational ensemble | LIGAND-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SUGAR BINDING | RESONANCE ENERGY-TRANSFER | D-glucose | protein function | INDUCED FIT | INTERNAL DYNAMICS | CHEMISTRY, MULTIDISCIPLINARY | guanidine hydrochloride | ISOTHERMAL TITRATION CALORIMETRY | GLUCOSE/GALACTOSE RECEPTOR | FLUORESCENT PROTEIN | D-galactose-binding protein | osmolyte-like stabilizing effect | CONFORMATIONAL SELECTION | Guanidine - chemistry | Protein Denaturation | Escherichia coli Proteins - genetics | Escherichia coli Proteins - metabolism | Monosaccharide Transport Proteins - chemistry | Protein Stability | Escherichia coli Proteins - chemistry | Monosaccharide Transport Proteins - metabolism | Molecular Dynamics Simulation | Amino Acid Substitution | Monosaccharide Transport Proteins - genetics | Binding | Fluorescence spectroscopy | Spectroscopy | Complementarity | Molecular structure | Structural stability | Guanidine | Fluorescence | Titration calorimetry | Chemoreception | Fluorescent indicators | Glucose | Compaction | Heat measurement | Proteins | Spectrum analysis | Dynamic stability | Calorimetry | Titration | Biosensors | Galactose | D-Galactose | d-galactose-binding protein">">d-galactose-binding protein | d-glucose">">d-glucose
Fluorescent label BADAN | Conformational ensemble | Osmolyte-like stabilizing effect | Protein function | Guanidine hydrochloride | D-glucose/D-galactose-binding protein | Protein conformers | protein conformers | fluorescent label BADAN | conformational ensemble | LIGAND-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SUGAR BINDING | RESONANCE ENERGY-TRANSFER | D-glucose | protein function | INDUCED FIT | INTERNAL DYNAMICS | CHEMISTRY, MULTIDISCIPLINARY | guanidine hydrochloride | ISOTHERMAL TITRATION CALORIMETRY | GLUCOSE/GALACTOSE RECEPTOR | FLUORESCENT PROTEIN | D-galactose-binding protein | osmolyte-like stabilizing effect | CONFORMATIONAL SELECTION | Guanidine - chemistry | Protein Denaturation | Escherichia coli Proteins - genetics | Escherichia coli Proteins - metabolism | Monosaccharide Transport Proteins - chemistry | Protein Stability | Escherichia coli Proteins - chemistry | Monosaccharide Transport Proteins - metabolism | Molecular Dynamics Simulation | Amino Acid Substitution | Monosaccharide Transport Proteins - genetics | Binding | Fluorescence spectroscopy | Spectroscopy | Complementarity | Molecular structure | Structural stability | Guanidine | Fluorescence | Titration calorimetry | Chemoreception | Fluorescent indicators | Glucose | Compaction | Heat measurement | Proteins | Spectrum analysis | Dynamic stability | Calorimetry | Titration | Biosensors | Galactose | D-Galactose | d-galactose-binding protein">">d-galactose-binding protein | d-glucose">">d-glucose
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 03/2019, Volume 125, pp. 244 - 255
pH-induced structural changes of the synthetic homopolypeptides poly-E, poly-K, poly-R, and intrinsically disordered proteins (IDPs) prothymosin α (ProTα) and...
POLYPEPTIDE-CHAINS | POLYMER SCIENCE | TERMINAL DOMAIN | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTHYMOSIN-ALPHA | STATE | THERMODYNAMIC PARAMETERS | PHASE-SEPARATION | HELIX-COIL TRANSITION | CONFORMATIONAL TRANSITIONS | SECONDARY STRUCTURE | CHEMISTRY, APPLIED | Polymerization | Histones | Amino acids | Hydrogen-ion concentration
POLYPEPTIDE-CHAINS | POLYMER SCIENCE | TERMINAL DOMAIN | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTHYMOSIN-ALPHA | STATE | THERMODYNAMIC PARAMETERS | PHASE-SEPARATION | HELIX-COIL TRANSITION | CONFORMATIONAL TRANSITIONS | SECONDARY STRUCTURE | CHEMISTRY, APPLIED | Polymerization | Histones | Amino acids | Hydrogen-ion concentration
Journal Article
Optical Materials, ISSN 0925-3467, 08/2014, Volume 36, Issue 10, pp. 1676 - 1679
The promising direction of the development of a modern glucometer is the construction of sensing element on the basis of stained (dyed) protein which changes...
Fluorescence | Fluorescent dye | Stability | Glucose | Biosensor | MUTANT | SPECIFICITY | MATERIALS SCIENCE, MULTIDISCIPLINARY | RESONANCE ENERGY-TRANSFER | SENSOR | FAMILY | ARCHAEON THERMOCOCCUS-LITORALIS | AFFINITY | CONSTRUCTION | OPTICS | Glucose metabolism | Dextrose | Detectors | Protein binding | Proteins | Binding | Dyes | Trehalose | Biosensors | Binding sites
Fluorescence | Fluorescent dye | Stability | Glucose | Biosensor | MUTANT | SPECIFICITY | MATERIALS SCIENCE, MULTIDISCIPLINARY | RESONANCE ENERGY-TRANSFER | SENSOR | FAMILY | ARCHAEON THERMOCOCCUS-LITORALIS | AFFINITY | CONSTRUCTION | OPTICS | Glucose metabolism | Dextrose | Detectors | Protein binding | Proteins | Binding | Dyes | Trehalose | Biosensors | Binding sites
Journal Article
The Journal of Physical Chemistry B, ISSN 1520-6106, 07/2011, Volume 115, Issue 29, pp. 9022 - 9032
The galactose/glucose-binding protein from E. coli (GGBP) is a 32 kDa protein possessing the typical two-domains structure of the ligand-binding proteins...
B: Macromolecules, Soft Matter | INTRINSIC FLUORESCENCE | SMOOTH-MUSCLE | TRANSPORT | CONFORMATIONAL-CHANGES | ESCHERICHIA-COLI | ACTIN-BOUND TROPOMYOSIN | CHEMISTRY, PHYSICAL | PERIPLASMIC RECEPTORS | TRANSITIONS | BIOSENSOR | AGGREGATION | Protein Denaturation - drug effects | Escherichia coli | Guanidine - pharmacology | Protein Conformation - drug effects | Mutant Proteins - genetics | Models, Molecular | Escherichia coli Proteins - metabolism | Mutant Proteins - metabolism | Hot Temperature | Mutant Proteins - chemistry | Protein Stability - drug effects | Biosensing Techniques | Escherichia coli Proteins - genetics | Glucose - metabolism | Protein Binding | Ligands | Monosaccharide Transport Proteins - chemistry | Mutation | Escherichia coli Proteins - chemistry | Monosaccharide Transport Proteins - metabolism | Amino Acid Substitution | Monosaccharide Transport Proteins - genetics | Proteins | Ligand binding (Biochemistry) | Research | Binding proteins | Structure | Protein binding | Stability | Amino acids | Constants | Affinity | Glucose | Monitoring | Guidelines
B: Macromolecules, Soft Matter | INTRINSIC FLUORESCENCE | SMOOTH-MUSCLE | TRANSPORT | CONFORMATIONAL-CHANGES | ESCHERICHIA-COLI | ACTIN-BOUND TROPOMYOSIN | CHEMISTRY, PHYSICAL | PERIPLASMIC RECEPTORS | TRANSITIONS | BIOSENSOR | AGGREGATION | Protein Denaturation - drug effects | Escherichia coli | Guanidine - pharmacology | Protein Conformation - drug effects | Mutant Proteins - genetics | Models, Molecular | Escherichia coli Proteins - metabolism | Mutant Proteins - metabolism | Hot Temperature | Mutant Proteins - chemistry | Protein Stability - drug effects | Biosensing Techniques | Escherichia coli Proteins - genetics | Glucose - metabolism | Protein Binding | Ligands | Monosaccharide Transport Proteins - chemistry | Mutation | Escherichia coli Proteins - chemistry | Monosaccharide Transport Proteins - metabolism | Amino Acid Substitution | Monosaccharide Transport Proteins - genetics | Proteins | Ligand binding (Biochemistry) | Research | Binding proteins | Structure | Protein binding | Stability | Amino acids | Constants | Affinity | Glucose | Monitoring | Guidelines
Journal Article
Journal of Fluorescence, ISSN 1053-0509, 1/2015, Volume 25, Issue 1, pp. 87 - 94
Changes of the characteristics of intrinsic tryptophan fluorescence of the wild type of D-galactose/D-glucose-binding protein from Escherichia coli (GGBPwt)...
Biochemistry, general | Biotechnology | Analytical Chemistry | Biomedicine | Microenvironment of tryptophan residues | Biophysics and Biological Physics | Tryptophan residue | Intrinsic fluorescence of proteins | Biomedicine general | THERMAL-STABILITY | MUTANT | CHEMISTRY, ANALYTICAL | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, PHYSICAL | SENSOR | CONFORMATIONAL DYNAMICS | TRANSPORT | RESONANCE | CONSTRUCTION | ENERGY-TRANSFER | PERIPLASMIC RECEPTORS | GLUCOSE/GALACTOSE | Catalytic Domain | Galactose - metabolism | Escherichia coli | Glucose - metabolism | Models, Molecular | Receptors, Cell Surface - metabolism | Spectrometry, Fluorescence | Tryptophan | Escherichia coli Proteins - metabolism | Receptors, Cell Surface - chemistry | Escherichia coli Proteins - chemistry | Proteins | Glucose metabolism | Analysis | Fluorescence | Chemical properties | Glucose | Dextrose | Protein binding | Binding | Residues | Quenching
Biochemistry, general | Biotechnology | Analytical Chemistry | Biomedicine | Microenvironment of tryptophan residues | Biophysics and Biological Physics | Tryptophan residue | Intrinsic fluorescence of proteins | Biomedicine general | THERMAL-STABILITY | MUTANT | CHEMISTRY, ANALYTICAL | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, PHYSICAL | SENSOR | CONFORMATIONAL DYNAMICS | TRANSPORT | RESONANCE | CONSTRUCTION | ENERGY-TRANSFER | PERIPLASMIC RECEPTORS | GLUCOSE/GALACTOSE | Catalytic Domain | Galactose - metabolism | Escherichia coli | Glucose - metabolism | Models, Molecular | Receptors, Cell Surface - metabolism | Spectrometry, Fluorescence | Tryptophan | Escherichia coli Proteins - metabolism | Receptors, Cell Surface - chemistry | Escherichia coli Proteins - chemistry | Proteins | Glucose metabolism | Analysis | Fluorescence | Chemical properties | Glucose | Dextrose | Protein binding | Binding | Residues | Quenching
Journal Article
Biophysics, ISSN 0006-3509, 3/2016, Volume 61, Issue 2, pp. 185 - 192
Osmolytes are molecules whose function, among others, is to balance the hydrostatic pressure between the intracellular and extracellular compartments....
osmolytes | osmotic stress |
osmolytes | osmotic stress |