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Flexibility–rigidity index for protein–nucleic acid flexibility and fluctuation analysis
Journal of Computational Chemistry, ISSN 0192-8651, 05/2016, Volume 37, Issue 14, pp. 1283 - 1295
Protein–nucleic acid complexes are important for many cellular processes including the most essential functions such as transcription and translation. For many...
thermal fluctuation | protein–nucleic acid complex | atomic flexibility | multiscale | protein-nucleic acid complex | CHAPERONIN GROEL | SINGLE-PARAMETER | CONTACT-NUMBER | CHEMISTRY, MULTIDISCIPLINARY | ELASTIC-NETWORK MODEL | STRUCTURAL FLEXIBILITY | FOLDED PROTEINS | ORDER PARAMETERS | DYNAMICS | NORMAL-MODE ANALYSIS | POLYMERASE-II | Nucleic Acids - chemistry | Algorithms | Proteins - chemistry | Analysis | Nucleic acids | Thermal fluctuation | Atomic flexibility | Multiscale
thermal fluctuation | protein–nucleic acid complex | atomic flexibility | multiscale | protein-nucleic acid complex | CHAPERONIN GROEL | SINGLE-PARAMETER | CONTACT-NUMBER | CHEMISTRY, MULTIDISCIPLINARY | ELASTIC-NETWORK MODEL | STRUCTURAL FLEXIBILITY | FOLDED PROTEINS | ORDER PARAMETERS | DYNAMICS | NORMAL-MODE ANALYSIS | POLYMERASE-II | Nucleic Acids - chemistry | Algorithms | Proteins - chemistry | Analysis | Nucleic acids | Thermal fluctuation | Atomic flexibility | Multiscale
Journal Article
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 01/2013, Volume 14, Issue 1, pp. 13 - 24
The nuclear lamina is an important structural determinant for the nuclear envelope as a whole, attaching chromatin domains to the nuclear periphery and...
CYTOPLASMIC DYNEIN | A-TYPE LAMIN | DROSOPHILA-MELANOGASTER | MEMBRANE PROTEIN | B-TYPE LAMINS | PRELAMIN-A | DISEASE PHENOTYPES | TRANSMEMBRANE PROTEINS | STRUCTURAL ORGANIZATION | RESTRICTIVE DERMOPATHY | CELL BIOLOGY | Cellular Senescence - genetics | Intermediate Filaments - genetics | Muscular Dystrophy, Animal - genetics | Chromatin | Humans | Nuclear Proteins - metabolism | Aging, Premature - genetics | Intermediate Filaments - metabolism | Animals | Cell Nucleus - metabolism | Cell Nucleus - genetics | Nuclear Lamina - metabolism | Gene Expression Regulation, Developmental | Nuclear Lamina - genetics | Mice | Embryonic Stem Cells | Mutation | Bone and Bones - abnormalities | Nuclear Proteins - genetics | Physiological aspects | Aging | Research | B cells | Health aspects | Membrane proteins
CYTOPLASMIC DYNEIN | A-TYPE LAMIN | DROSOPHILA-MELANOGASTER | MEMBRANE PROTEIN | B-TYPE LAMINS | PRELAMIN-A | DISEASE PHENOTYPES | TRANSMEMBRANE PROTEINS | STRUCTURAL ORGANIZATION | RESTRICTIVE DERMOPATHY | CELL BIOLOGY | Cellular Senescence - genetics | Intermediate Filaments - genetics | Muscular Dystrophy, Animal - genetics | Chromatin | Humans | Nuclear Proteins - metabolism | Aging, Premature - genetics | Intermediate Filaments - metabolism | Animals | Cell Nucleus - metabolism | Cell Nucleus - genetics | Nuclear Lamina - metabolism | Gene Expression Regulation, Developmental | Nuclear Lamina - genetics | Mice | Embryonic Stem Cells | Mutation | Bone and Bones - abnormalities | Nuclear Proteins - genetics | Physiological aspects | Aging | Research | B cells | Health aspects | Membrane proteins
Journal Article
Journal of Chemical Physics, ISSN 0021-9606, 11/2013, Volume 139, Issue 19, p. 194109
The emerging complexity of large macromolecules has led to challenges in their full scale theoretical description and computer simulation. Multiscale...
MOLECULAR-DYNAMICS | ENERGY | ELECTROSTATIC FORCES | SINGLE-PARAMETER | MEMBRANE CURVATURE | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CHEMISTRY, PHYSICAL | PROTON TRANSPORT | MECHANISMS | ELASTIC NETWORK MODELS | POISSON-BOLTZMANN EQUATION | PROTEIN FLEXIBILITY | Models, Molecular | Protein Conformation | Proteins - metabolism | Proteins - chemistry | Molecular Dynamics Simulation | Residues | Construction | Parameters | Computer simulation | Shear modulus | Computational fluid dynamics | Macromolecules | Fluid flow | Atomic properties | Elasticity | Rigidity | Flexibility | Model accuracy | Complexity | Proteins | Interpolation | Organic chemistry | Solvation | Boltzmann transport equation | Chemical potential | Computing time | Electrostatics | Continuity (mathematics) | PROTEIN STRUCTURE | DEGREES OF FREEDOM | FLEXIBILITY | INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY | ALGORITHMS | POTENTIALS | BOLTZMANN EQUATION | FUNCTIONS | INTERACTIONS | SOLVATION | ACCURACY | COMPUTERIZED SIMULATION | ELASTICITY | INTERPOLATION | HAMILTONIANS | PROTEINS | EFFICIENCY | MATHEMATICAL METHODS AND COMPUTING | Theoretical Methods and Algorithms
MOLECULAR-DYNAMICS | ENERGY | ELECTROSTATIC FORCES | SINGLE-PARAMETER | MEMBRANE CURVATURE | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CHEMISTRY, PHYSICAL | PROTON TRANSPORT | MECHANISMS | ELASTIC NETWORK MODELS | POISSON-BOLTZMANN EQUATION | PROTEIN FLEXIBILITY | Models, Molecular | Protein Conformation | Proteins - metabolism | Proteins - chemistry | Molecular Dynamics Simulation | Residues | Construction | Parameters | Computer simulation | Shear modulus | Computational fluid dynamics | Macromolecules | Fluid flow | Atomic properties | Elasticity | Rigidity | Flexibility | Model accuracy | Complexity | Proteins | Interpolation | Organic chemistry | Solvation | Boltzmann transport equation | Chemical potential | Computing time | Electrostatics | Continuity (mathematics) | PROTEIN STRUCTURE | DEGREES OF FREEDOM | FLEXIBILITY | INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY | ALGORITHMS | POTENTIALS | BOLTZMANN EQUATION | FUNCTIONS | INTERACTIONS | SOLVATION | ACCURACY | COMPUTERIZED SIMULATION | ELASTICITY | INTERPOLATION | HAMILTONIANS | PROTEINS | EFFICIENCY | MATHEMATICAL METHODS AND COMPUTING | Theoretical Methods and Algorithms
Journal Article
The Journal of Chemical Physics, ISSN 0021-9606, 06/2016, Volume 144, Issue 23, p. 234106
Flexibility-rigidity index (FRI) has been developed as a robust, accurate, and efficient method for macromolecular thermal fluctuation analysis and B-factor...
PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | DYNAMICS | CHEMISTRY, PHYSICAL | PREDICTIONS | NORMAL-MODE ANALYSIS | PROTEINS | MOTIONS | Proteins | Formulations | Variations | Rigidity | Flexibility | Quantitative Biology - Biomolecules
PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | DYNAMICS | CHEMISTRY, PHYSICAL | PREDICTIONS | NORMAL-MODE ANALYSIS | PROTEINS | MOTIONS | Proteins | Formulations | Variations | Rigidity | Flexibility | Quantitative Biology - Biomolecules
Journal Article
BBA - Proteins and Proteomics, ISSN 1570-9639, 2011, Volume 1814, Issue 8, pp. 969 - 976
Proteins rely on flexibility to respond to environmental changes, ligand binding and chemical modifications. Potentially, a perturbation that changes the...
Ligand binding | Protein stability | Flexibility | Protein affinity | LIGAND-BINDING | THERMODYNAMIC STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROPHOBIC CORE SUBSTITUTIONS | MUSCLE TROPONIN-C | BIOPHYSICS | DIHYDROFOLATE-REDUCTASE | 2-STATE PROTEINS | INTERMOLECULAR INTERACTIONS | ENERGY LANDSCAPE | RECEPTOR-BINDING | SH3 DOMAIN
Ligand binding | Protein stability | Flexibility | Protein affinity | LIGAND-BINDING | THERMODYNAMIC STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROPHOBIC CORE SUBSTITUTIONS | MUSCLE TROPONIN-C | BIOPHYSICS | DIHYDROFOLATE-REDUCTASE | 2-STATE PROTEINS | INTERMOLECULAR INTERACTIONS | ENERGY LANDSCAPE | RECEPTOR-BINDING | SH3 DOMAIN
Journal Article
Journal of Computational Chemistry, ISSN 0192-8651, 12/2009, Volume 30, Issue 16, pp. 2785 - 2791
We describe the testing and release of AutoDock4 and the accompanying graphical user interface AutoDockTools. AutoDock4 incorporates limited flexibility in the...
protein flexibility | covalent ligands | computer‐aided drug design | AutoDock | computational docking | ALGORITHMS | FLEXIBLE LIGANDS | SUCCESSES | PROTEINS | computer-aided drug design | CHEMISTRY, MULTIDISCIPLINARY | CHALLENGES | Models, Molecular | Protein Binding | Ligands | Software | Proteins - metabolism
protein flexibility | covalent ligands | computer‐aided drug design | AutoDock | computational docking | ALGORITHMS | FLEXIBLE LIGANDS | SUCCESSES | PROTEINS | computer-aided drug design | CHEMISTRY, MULTIDISCIPLINARY | CHALLENGES | Models, Molecular | Protein Binding | Ligands | Software | Proteins - metabolism
Journal Article
Cellular and Molecular Life Sciences, ISSN 1420-682X, 07/2009, Volume 66, Issue 14, pp. 2231 - 2247
Proteins are dynamic entities, and they possess an inherent flexibility that allows them to function through molecular interactions within the cell, among...
Protein-ligand interactions | Entropy | Protein dynamics | Intrinsically disordered proteins | Flexible protein recognition model | Protein flexibility | LIMITED PROTEOLYSIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | INTRINSICALLY UNSTRUCTURED PROTEINS | STRUCTURAL-CHARACTERIZATION | MOLECULAR-DYNAMICS SIMULATION | CELL BIOLOGY | CIS-TRANS ISOMERIZATION | PHYSIOLOGICAL CONDITIONS | ORDER PARAMETERS | BACKBONE CONFORMATIONAL ENTROPY | Thermodynamics | Proteins - metabolism | Models, Molecular | Protein Binding | Ligands | Protein Conformation | Structure-Activity Relationship | Proteins - chemistry | Binding Sites | Proteins | Analysis | Protein binding | Studies | Molecular biology
Protein-ligand interactions | Entropy | Protein dynamics | Intrinsically disordered proteins | Flexible protein recognition model | Protein flexibility | LIMITED PROTEOLYSIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | INTRINSICALLY UNSTRUCTURED PROTEINS | STRUCTURAL-CHARACTERIZATION | MOLECULAR-DYNAMICS SIMULATION | CELL BIOLOGY | CIS-TRANS ISOMERIZATION | PHYSIOLOGICAL CONDITIONS | ORDER PARAMETERS | BACKBONE CONFORMATIONAL ENTROPY | Thermodynamics | Proteins - metabolism | Models, Molecular | Protein Binding | Ligands | Protein Conformation | Structure-Activity Relationship | Proteins - chemistry | Binding Sites | Proteins | Analysis | Protein binding | Studies | Molecular biology
Journal Article
Journal of Medicinal Chemistry, ISSN 0022-2623, 10/2008, Volume 51, Issue 20, pp. 6237 - 6255
CHEMISTRY, MEDICINAL | SIDE-CHAIN FLEXIBILITY | RESOLUTION CRYSTAL-STRUCTURE | LIGAND-BINDING | PROTEIN-COUPLED RECEPTOR | SCHISTOSOMA-MANSONI SM14 | AUTOMATED DOCKING | X-RAY-DIFFRACTION | MOLECULAR-DYNAMICS SIMULATIONS | ENERGY PERTURBATION METHOD | ALDOSE REDUCTASE | Animals | Proteins - metabolism | Computer Simulation | Humans | Drug Design | Pharmaceutical Preparations - chemistry | Nuclear Magnetic Resonance, Biomolecular | Crystallography, X-Ray | Proteins - chemistry | Drug Evaluation, Preclinical
Journal Article