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Journal Article
Protein Science, ISSN 0961-8368, 07/2014, Volume 23, Issue 7, pp. 897 - 905
The folding of a multi‐domain trimeric α‐helical membrane protein, Escherichia coli inner membrane protein AcrB, was investigated. AcrB contains both a... 
membrane protein | oligomer | multi‐domain | protein folding | Membrane protein | Multi-domain | Oligomer | Protein folding | RENATURATION | MECHANISM | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DENATURATION | MIXED MICELLES | MULTIDRUG EFFLUX PUMP | IN-VITRO | multi-domain | TRANSPORT PROTEIN | FREE-ENERGY | Protein Structure, Tertiary | Phenylalanine - metabolism | Protein Structure, Secondary | Multidrug Resistance-Associated Proteins - drug effects | Protein Multimerization | Multidrug Resistance-Associated Proteins - chemistry | Protein Refolding | Models, Molecular | Escherichia coli Proteins - metabolism | Escherichia coli - chemistry | Tryptophan - metabolism | Urea - chemistry | Sodium Dodecyl Sulfate - pharmacology | Protein Denaturation | Escherichia coli Proteins - genetics | Multidrug Resistance-Associated Proteins - genetics | Kinetics | Mutation | Escherichia coli Proteins - chemistry | Escherichia coli Proteins - drug effects | Circular Dichroism | Multidrug Resistance-Associated Proteins - metabolism | Urea - pharmacology | Studies | Spectrum analysis | Bacteriology | Spectroscopy | Sodium lauryl sulfate | Denaturation | Fluorescence | Pollution monitoring | Trimers | Secondary structure | Monomers | Constraining | Circular dichroism | Membrane proteins | Sodium dodecyl sulfate | Domains | Proteins | Urea | Sodium | E coli | Dichroism | Protein structure
Journal Article
Structure, ISSN 0969-2126, 11/2017, Volume 25, Issue 11, pp. 1740 - 1750.e2
A major cause of visual impairment, corneal dystrophies result from accumulation of protein deposits in the cornea. One of the proteins involved is... 
extracellular matrix protein | cysteine-rich CROPT domain | multi-domain protein | pathological mutants | crystal structure | corneal dystrophy | fasciclin FAS1 domain | GENOTYPE-PHENOTYPE CORRELATION | WILD-TYPE | EXON 14 | KERATO-EPITHELIN MUTATIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | BIOPHYSICS | STRUCTURE VALIDATION | BETA-IG-H3 | CHINESE PATIENTS | BIGH3 GENE-MUTATIONS | LATTICE | ASSOCIATION | Protein Aggregates | Humans | Integrins - chemistry | Corneal Dystrophies, Hereditary - genetics | Integrins - genetics | Crystallography, X-Ray | Transforming Growth Factor beta - chemistry | Integrins - metabolism | Corneal Dystrophies, Hereditary - pathology | Cloning, Molecular | HEK293 Cells | Protein Interaction Domains and Motifs | Binding Sites | Protein Aggregation, Pathological - genetics | Extracellular Matrix Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Extracellular Matrix Proteins - chemistry | Gene Expression | Genetic Vectors - chemistry | Extracellular Matrix Proteins - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Corneal Dystrophies, Hereditary - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Transforming Growth Factor beta - genetics | Protein Conformation, beta-Strand | Protein Binding | Mutation | Transforming Growth Factor beta - metabolism | Protein Aggregation, Pathological - metabolism
Journal Article
Methods, ISSN 1046-2023, 04/2017, Volume 118-119, pp. 119 - 136
Recent advances in RNA sequencing technologies have greatly expanded our knowledge of the RNA landscape in cells, often with spatiotemporal resolution. These... 
RNA-protein complex | Molecular dynamics | Small angle scattering | Integrated structural biology | Nuclear magnetic resonance | Multi-domain proteins | DOUBLE-STRANDED-RNA | SMALL-ANGLE SCATTERING | NUCLEIC ACID INTERACTIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MACROMOLECULAR NMR-SPECTROSCOPY | BIOCHEMICAL RESEARCH METHODS | SPLICING FACTOR U2AF65 | U4/U6.U5 TRI-SNRNP | MESSENGER-RNA | SINGLE-NUCLEOTIDE RESOLUTION | CRYO-EM STRUCTURE | VTS1P SAM DOMAIN | RNA-Binding Proteins - genetics | Humans | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | RNA - genetics | Crystallography, X-Ray - methods | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Base Sequence | Ribonucleoproteins - genetics | Protein Interaction Domains and Motifs | Ribonucleoproteins - chemistry | Nucleic Acid Conformation | Binding Sites | RNA - metabolism | Computational Biology - methods | RNA-Binding Proteins - chemistry | Ribonucleoproteins - metabolism | Drosophila Proteins - chemistry | DNA-Binding Proteins - genetics | RNA - chemistry | DNA-Binding Proteins - chemistry | Molecular Dynamics Simulation | Splicing Factor U2AF - genetics | Animals | Nuclear Magnetic Resonance, Biomolecular - methods | Protein Binding | Fluorescence Resonance Energy Transfer - methods | Splicing Factor U2AF - chemistry | Drosophila Proteins - genetics | RNA-Binding Proteins - metabolism | Splicing Factor U2AF - metabolism | RNA | Molecular biology
Journal Article
Chemical Physics, ISSN 0301-0104, 10/2018, Volume 514, pp. 95 - 105
Entropy–enthalpy compensation is observed in many reactions, particularly for polymeric biomolecules that often involve large changes in entropy and enthalpy.... 
Entropy-enthalpy compensation | Protein stability | Coarse-grained simulations | Protein folding | Multi-domain proteins | Unfolded state | MULTIDOMAIN PROTEINS | STABILITY | UBIQUITIN | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | ENERGY LANDSCAPE THEORY | CHEMISTRY, PHYSICAL | GLYCOSYLATION | DETERMINES | FOLDING FUNNELS | INCREASE | DYNAMICS | Proteins | Thermodynamics
Journal Article
Protein Science, ISSN 0961-8368, 10/2018, Volume 27, Issue 10, pp. 1780 - 1796
Spleen tyrosine kinase (Syk) is an essential player in immune signaling through its ability to couple multiple classes of membrane immunoreceptors to... 
spleen tyrosine kinase (Syk) | tyrosine phosphorylation allostery | entropic allostery | multistate equilibrium with isomerization | regulation of protein–protein interaction | multi‐domain ensemble thermodynamics | NMR chemical shift difference analysis | tandem SH2 domain (tSH2) | doubly phosphorylated immunoreceptor tyrosine‐based activation motif (dp‐ITAM) | isothermal titration calorimetry model and data analysis | doubly phosphorylated immunoreceptor tyrosine-based activation motif (dp-ITAM) | multi-domain ensemble thermodynamics | LIGAND-BINDING | SPECIFICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 3-KINASE SH2 DOMAIN | TANDEM SH2 | ISOTHERMAL TITRATION CALORIMETRY | PROTEIN INTERACTIONS | NMR | regulation of protein-protein interaction | STRUCTURAL BASIS | CELL ANTIGEN RECEPTOR | STRESS GRANULES | Proteins | Tyrosine | Thermodynamics | Analysis | Isomerization | Phenols | Information management | Protein-protein interactions | Phosphorylation | Nuclear magnetic resonance--NMR | Enthalpy | Intracellular signalling | Entropy | Kinases | Receptors | Allosteric properties | Protein-tyrosine kinase | Binding | Spleen | Titration calorimetry | Free energy | Domains | Organic chemistry | Chemical equilibrium | Calorimetry | Affinity | Syk protein | Titration | Immunoreceptor tyrosine-based activation motif | Protein interaction | Full‐Length Papers | Full‐Length Paper
Journal Article
FEBS Letters, ISSN 0014-5793, 2010, Volume 584, Issue 16, pp. 3620 - 3624
Journal Article