يعرض 1 - 8 نتائج من 8 نتيجة بحث عن '"real-time NMR"', وقت الاستعلام: 1.25s تنقيح النتائج
  1. 1
    Determination of intracellular protein–ligand binding affinity by competition binding in-cell NMR

    المؤلفون: Lucia Banci, Matteo Pennestri, Letizia Barbieri, Enrico Luchinat, Alessio Nocentini, Matteo Cremonini, Claudiu T. Supuran

    المساهمون: Luchinat, Enrico, Barbieri, Letizia, Cremonini, Matteo, Pennestri, Matteo, Nocentini, Alessio, Supuran, Claudiu T, Banci, Lucia

    المصدر: Acta Crystallographica. Section D, Structural Biology
    Acta Crystallographica Section D Structural Biology

    مصطلحات موضوعية: carbonic anhydrase inhibitors, Magnetic Resonance Spectroscopy, Carbonic anhydrase II, Cell, 010402 general chemistry, Binding, Competitive, Carbonic Anhydrase II, 01 natural sciences, competition binding, Structure-Activity Relationship, bioreactor, 03 medical and health sciences, Structural Biology, medicine, Humans, carbonic anhydrase inhibitor, 030304 developmental biology, Sulfonamides, 0303 health sciences, bioreactor, carbonic anhydrase inhibitors, competition binding, in-cell NMR, real-time NMR, in-cell NMR, Chemistry, real-time NMR, Nuclear magnetic resonance spectroscopy, Affinities, In vitro, 0104 chemical sciences, Dissociation constant, medicine.anatomical_structure, Biophysics, Thermodynamics, Target protein, Ccp4, Intracellular, Protein Binding

    وصف الملف: ELETTRONICO

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c41415cd86da59f735c68bc7252d9a3Test
    https://doi.org/10.1107/s2059798321009037Test


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  2. 2
    Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

    المؤلفون: Enrico Luchinat, Letizia Barbieri

    المساهمون: Barbieri, Letizia, Luchinat, Enrico

    المصدر: Journal of Visualized Experiments

    مصطلحات موضوعية: 0301 basic medicine, Magnetic Resonance Spectroscopy, ligand binding, General Chemical Engineering, carbonic anhydrase, kinetic, Context (language use), Ligands, Protein oxidation, General Biochemistry, Genetics and Molecular Biology, bioreactor, 03 medical and health sciences, Bioreactors, 0302 clinical medicine, Bioreactor, Humans, protocol, in-cell NMR, bioreactor, protocol, real-time NMR, nuclear magnetic resonance, kinetics, ligand binding, carbonic anhydrase, superoxide dismutase, General Immunology and Microbiology, in-cell NMR, Chemistry, General Neuroscience, real-time NMR, Proteins, Ligand (biochemistry), superoxide dismutase, NMR spectra database, nuclear magnetic resonance, Chemical species, 030104 developmental biology, 030220 oncology & carcinogenesis, Biophysics, Protein folding, Protein ligand

    وصف الملف: ELETTRONICO

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23772b59c49e607e266cc19f33f0cc40Test
    https://doi.org/10.3791/62323Test


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  3. 3
    Aggregation pathways of human γ D crystallin induced by metal ions revealed by time dependent methods

    المؤلفون: Leidys French-Pacheco, Arline Fernández-Silva, Carlos Amero, Lina Rivillas-Acevedo

    المصدر: PeerJ, Vol 8, p e9178 (2020)
    PeerJ

    مصطلحات موضوعية: Metal ions in aqueous solution, Biophysics, lcsh:Medicine, chemistry.chemical_element, Zinc, Protein aggregation, Biochemistry, General Biochemistry, Genetics and Molecular Biology, Metal, Aggregation, 03 medical and health sciences, Dynamic light scattering, Crystallin, Human gamma-D crystallin, 030304 developmental biology, 0303 health sciences, Cataracts, Chemistry, General Neuroscience, lcsh:R, 030302 biochemistry & molecular biology, General Medicine, Real-time NMR, Crystallins, Fluorescence, visual_art, visual_art.visual_art_medium, Turbidimetry, General Agricultural and Biological Sciences, Copper

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c417e81462a1d3b5f0bdb973f3d10839Test
    https://doi.org/10.7717/peerj.9178Test


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  4. 4
    Photoswitching of Green mEos2 by Intense 561 nm Light Perturbs Efficient Green-to-Red Photoconversion in Localization Microscopy

    المؤلفون: Daniel Thédié, Dominique Bourgeois, Virgile Adam, Romain Berardozzi

    المساهمون: Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

    المصدر: Journal of Physical Chemistry Letters
    Journal of Physical Chemistry Letters, American Chemical Society, 2017, 8 (18), pp.4424-4430. ⟨10.1021/acs.jpclett.7b01701⟩
    Journal of Physical Chemistry Letters, 2017, 8 (18), pp.4424-4430. ⟨10.1021/acs.jpclett.7b01701⟩

    مصطلحات موضوعية: 0301 basic medicine, Fast mixing, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Analytical chemistry, Real-time NMR, Fluorescence, Photobleaching, 03 medical and health sciences, 030104 developmental biology, SOFAST, Microscopy, Biophysics, General Materials Science, Photoactivated localization microscopy, Protein folding, Physical and Theoretical Chemistry, β2-microglobulin

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bf32be7ef135e7ecf01e36f976a1ab2Test
    https://hal.archives-ouvertes.fr/hal-01592521Test


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  5. 5
    Optimized fast mixing device for real-time NMR applications

    المؤلفون: Rémi Franco, Bernhard Brutscher, Adrien Favier, Paul Schanda

    المساهمون: Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

    المصدر: Journal of Magnetic Resonance
    Journal of Magnetic Resonance, 2017, 281, pp.125-129. ⟨10.1016/j.jmr.2017.05.016⟩
    Journal of Magnetic Resonance, Elsevier, 2017, 281, pp.125-129. ⟨10.1016/j.jmr.2017.05.016⟩

    مصطلحات موضوعية: 0301 basic medicine, Nuclear and High Energy Physics, Biophysics, Analytical chemistry, 010402 general chemistry, 01 natural sciences, Biochemistry, Article, law.invention, 03 medical and health sciences, law, Transverse relaxation-optimized spectroscopy, Protein folding, Mixing (physics), β2-microglobulin, Fast mixing, Spectrometer, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Homogeneity (statistics), Injector, Folding (DSP implementation), Real-time NMR, Condensed Matter Physics, 0104 chemical sciences, Characterization (materials science), Magnetic field, 030104 developmental biology, SOFAST

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9d1e3b5216d41246251ec98e0ab144aTest
    https://hal.science/hal-01538754Test


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  6. 6
    Monitoring fibril formation of the N-terminal domain of PABPN1 carrying an alanine repeat by tryptophan fluorescence and real-time NMR

    المؤلفون: Elisabeth Schwarz, Rolf Sachs, Jochen Balbach, Mirko Sackewitz, Julia Rohrberg, Grit Lodderstedt

    المصدر: FEBS Letters. 582:1587-1592

    مصطلحات موضوعية: Repetitive Sequences, Amino Acid, Amyloid, Molecular Sequence Data, Kinetics, Biophysics, Fibril formation, macromolecular substances, Poly-alanine, Fibril, Poly(A)-Binding Protein II, Biochemistry, Fluorescence, Fluorescence spectroscopy, Protein structure, Structural Biology, Tryptophan fluorescence, Genetics, Humans, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Alanine, Chemistry, PABPN1, Binding protein, Tryptophan, Cell Biology, Nuclear magnetic resonance spectroscopy, Real-time NMR, Trinucleotide expansion, Recombinant Proteins, Protein Structure, Tertiary, Crystallography

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e17fc98b0956f1323ddc2edc0ddbfc0Test
    https://doi.org/10.1016/j.febslet.2008.04.002Test


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  7. 7
    Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments

    المؤلفون: Canet, D, Lyon, CE, Scheek, RM, Robillard, GT, Dobson, CM, Hore, PJ, van Nuland, NAJ, Lyon, Charles E., Dobson, Christopher M., Hore, Peter J.

    المساهمون: Groningen Biomolecular Sciences and Biotechnology, Molecular Dynamics, Enzymology, Faculty of Science and Engineering

    المصدر: Journal of Molecular Biology, 330(2), 397-407. Academic Press

    مصطلحات موضوعية: Models, Molecular, Protein Denaturation, Protein Folding, RESTRAINED MOLECULAR-DYNAMICS, Globular protein, Photochemistry, Fluorescence Polarization, DISEASE, Bacterial Proteins, Structural Biology, Native state, AMINO-ACIDS, CONTAINING PHOSPHOCARRIER PROTEIN, Hydrophobic collapse, Phosphoenolpyruvate Sugar Phosphotransferase System, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, chemistry.chemical_classification, Quenching (fluorescence), photo-CIDNP, CIDNP, Chemistry, Tryptophan, real-time NMR, INTERMEDIATE, Crystallography, Kinetics, HISTIDINE, HIGH-RESOLUTION STRUCTURE, non-native contacts, Biophysics, Mutagenesis, Site-Directed, TRIPLET, Protein folding, fluorescence, HEN LYSOZYME, Fluorescence anisotropy

    وصف الملف: application/pdf

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da82f9d4a827a3cbca7b53b260f3d944Test
    https://pubmed.ncbi.nlm.nih.gov/12823977Test


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  8. 8
    Caught in the Act: ATP hydrolysis of an ABC-multidrug transporter followed by real-time magic angle spinning NMR

    المؤلفون: Saroj Velamakanni, Ute A. Hellmich, Clemens Glaubitz, Winfried Haase, Hendrik W. van Veen

    المصدر: FEBS Letters. (23-24):3557-3562

    مصطلحات موضوعية: Time Factors, Biophysics, ATP-binding cassette transporter, Biochemistry, Solid-state NMR, chemistry.chemical_compound, Adenosine Triphosphate, Bacterial Proteins, Structural Biology, ATP hydrolysis, Genetics, Magic angle spinning, ABC-transporter, 31P NMR, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, POPC, biology, Chemistry, Hydrolysis, Lactococcus lactis, Phosphorus Isotopes, Cell Biology, Real-time NMR, biology.organism_classification, Kinetics, Microscopy, Electron, Crystallography, Solid-state nuclear magnetic resonance, Cyclic nucleotide-binding domain, Multidrug Resistance-Associated Proteins, Adenosine triphosphate

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edb720d0a9b7cf79231d6e2442ff5489Test


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