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Journal of Physical Chemistry B, ISSN 1520-6106, 10/2018, Volume 122, Issue 40, pp. 9314 - 9323
Hydrogen deuterium exchange (HDX) experiments are widely used in studies of protein dynamics. To predict the propensity of amide hydrogens for exchange with... 
CYTOCHROME-C | NATIVE PROTEINS | FOLDED PROTEINS | PROTECTION FACTORS | CHEMISTRY, PHYSICAL | HYDROGEN/DEUTERIUM EXCHANGE | CONFORMATIONAL DYNAMICS | MOLECULAR-DYNAMICS SIMULATIONS | TRYPSIN-INHIBITOR | MASS-SPECTROMETRY | SOLVENT ACCESSIBILITY
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2017, Volume 12, Issue 9, pp. e0180905 - e0180905
Proteins associated with neurodegenerative diseases are highly pleiomorphic and may adopt an all-a-helical fold in one environment, assemble into... 
ALPHA-SYNUCLEIN OLIGOMERS | ATOMIC-FORCE MICROSCOPY | SOLID-STATE NMR | SODIUM DODECYL-SULFATE | MULTIDISCIPLINARY SCIENCES | PARTIALLY FOLDED STRUCTURE | PAIRED HELICAL FILAMENTS | AMYLOID-BETA-PROTEIN | C-TERMINAL THREONINE | INDUCED CONFORMATIONAL-CHANGES | HUMAN PRION PROTEIN | Protein Aggregates | Protein Structure, Secondary | Humans | Protein Multimerization | Models, Molecular | tau Proteins - metabolism | PrPSc Proteins - chemistry | Protein Folding | tau Proteins - chemistry | PrPSc Proteins - genetics | alpha-Synuclein - chemistry | PrPSc Proteins - metabolism | Animals | tau Proteins - genetics | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - metabolism | Protein Domains | alpha-Synuclein - genetics | Amyloid beta-Peptides - chemistry | Protein Stability | alpha-Synuclein - metabolism | Electrons | Hydrogen-Ion Concentration | Protein folding | Physiological aspects | Nervous system | Development and progression | Degeneration | Genetic aspects | Research | Coils | Amyloidogenesis | Backbone | Rate constants | Agglomeration | Synuclein | pH effects | Neuromodulation | Modulators | Proteins | Oligomers | Fibrillogenesis | Pathways | Chirality | Chemical bonds | Catalysis | Prion protein | Dimerization | Folding | Linkages | Polypeptides | Incubation | Neurodegenerative diseases | Tertiary structure | Polymerization | Shielding | Secondary structure | Density distribution | Neurological diseases | Chemistry | Tensors | Propagation (polymerization) | Aggregates | Tau protein | Prions | Morphology | β-Amyloid | Dimers | Mutation | Protein structure | Index Medicus
Journal Article
Structure, ISSN 0969-2126, 11/2017, Volume 25, Issue 11, pp. 1687 - 1696.e4
The evolution of protein-coding genes from noncoding DNA is emerging as a source of molecular innovation in biology. Studies of random sequence libraries,... 
conformational specificity | amyloid oligomer | molten globule | de novo protein | protein folding | partially folded protein | structural evolution | de novo protein-coding gene | NETWORK | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | NATIVELY UNFOLDED PROTEINS | MOLTEN GLOBULE | BIOPHYSICS | FOLDED PROTEINS | SEQUENCE | GENES | MASS | SURFACE | SECONDARY STRUCTURE | BINDING | Protein Biosynthesis | Saccharomyces cerevisiae - genetics | Protein Multimerization | Saccharomyces cerevisiae - metabolism | Thermodynamics | DNA, Intergenic - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein Denaturation | Recombinant Proteins - metabolism | Amino Acid Sequence | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | DNA, Intergenic - genetics | Protein Folding | DNA, Intergenic - chemistry | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Kinetics | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Oligomers | Noncoding DNA | Genetic research | Evolutionary biology | Denaturation | Index Medicus | De novo protein
Journal Article
FEBS Journal, ISSN 1742-464X, 08/2013, Volume 280, Issue 16, pp. 3810 - 3821
The twin‐arginine translocation (Tat) system transports folded proteins across the plasma membrane in bacteria, and heterologous proteins can be exported by... 
GFP | TatAdCd | scherichia coli | acillus subtilis | green fluorescent protein | twin arginine translocation (Tat) signal peptide | green fluorescent protein (GFP) | Escherichia coli | Bacillus subtilis TatAdCd | Escherichiacoli | BIOCHEMISTRY & MOLECULAR BIOLOGY | Bacillussubtilis | EXPORT | QUALITY-CONTROL | RECOVERY | GREEN FLUORESCENT PROTEIN | FOLDED PROTEINS | TAT PATHWAY | PERIPLASM | PROMOTER | EXPRESSION | SUBUNIT | Recombinant Fusion Proteins - biosynthesis | Recombinant Proteins - metabolism | Batch Cell Culture Techniques | Oxidoreductases, N-Demethylating - genetics | Oxidoreductases, N-Demethylating - secretion | Bacterial Proteins - genetics | Green Fluorescent Proteins - genetics | Recombinant Proteins - genetics | Recombinant Fusion Proteins - chemistry | Fermentation | Protein Sorting Signals | Oxidoreductases, N-Demethylating - chemistry | Green Fluorescent Proteins - biosynthesis | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | Recombinant Fusion Proteins - secretion | Bacterial Proteins - metabolism | Membrane Transport Proteins - metabolism | Escherichia coli - growth & development | Green Fluorescent Proteins - secretion | Kinetics | Oxidoreductases, N-Demethylating - biosynthesis | Escherichia coli - ultrastructure | Bacillus subtilis - metabolism | Arginine | Recombinant proteins | Signal transduction | E coli | Peptides | Gene expression | Bacterial proteins | Index Medicus
Journal Article
Applied and Environmental Microbiology, ISSN 0099-2240, 02/2011, Volume 77, Issue 3, pp. 871 - 881
Journal Article
Journal Article
Amino Acids, ISSN 0939-4451, 11/2011, Volume 41, Issue 5, pp. 1233 - 1245
The G170R variant of the alanine:glyoxylate aminotransferase (AGT) is the most common pathogenic allele associated to primary hyperoxaluria type I (PH1),... 
Life Sciences | Biochemistry, general | Analytical Chemistry | Life Sciences, general | Molecular chaperones | Neurobiology | Proteomics | Biochemical Engineering | Alanine:glyoxylate aminotransferase | Partially folded states | Protein kinetic stability | Primary hyperoxaluria type 1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DIFFERENTIAL SCANNING CALORIMETRY | TRANSITION-STATE | IMPORT | MOLTEN GLOBULE | ASPARTATE-AMINOTRANSFERASE | ALANINEGLYOXYLATE AMINOTRANSFERASE | ALPHA-LACTALBUMIN | ALANINE-GLYOXYLATE AMINOTRANSFERASE | HUMAN-LIVER ALANINE | Cell Line | HSC70 Heat-Shock Proteins - genetics | Protein Unfolding | Transaminases - genetics | HSC70 Heat-Shock Proteins - metabolism | Humans | Mitochondrial Proteins - genetics | Transaminases - chemistry | Hyperoxaluria, Primary - enzymology | Protein Transport | Hyperoxaluria, Primary - genetics | HSC70 Heat-Shock Proteins - chemistry | Mitochondrial Proteins - metabolism | Hyperoxaluria, Primary - metabolism | Mitochondrial Proteins - chemistry | Transaminases - metabolism | HSP90 Heat-Shock Proteins - chemistry | HSP90 Heat-Shock Proteins - metabolism | Protein Binding | HSP90 Heat-Shock Proteins - genetics | Kinetics | Phosphates | Proteins | Magneto-electric machines | Analysis | Escherichia coli | Heat shock proteins | Amino acids | Machinery | Trapping | Stability | Reaction kinetics | Folding | Index Medicus
Journal Article
Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, 03/2019, Volume 37, Issue 5, pp. 1204 - 1219
We dissect the protein-protein interfaces into water preservation (WP), water hydration (WH) and water dehydration (WD) sites by comparing the water-mediated... 
water bridges | conformational change | hydrogen bonds | interface waters | protein-protein interfaces | protein–protein interfaces | MEDIATED INTERACTIONS | RECOGNITION | DOCKING | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDRATION | MOLECULES | PREDICTION | ORGANIZATION | REFINEMENT | BIOPHYSICS | FOLDED PROTEINS | SECONDARY STRUCTURE
Journal Article