المؤلفون: Stéphane Pezennec, Françoise Nau, Yann Desfougères, Franck Artzner, Valérie Lechevalier

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Biophysique, Institut de Physique de Rennes (IPR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)

المصدر: Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry, 2008, 56 (13), pp.5120-8. ⟨10.1021/jf703715j⟩
Journal of Agricultural and Food Chemistry, American Chemical Society, 2008, 56 (13), pp.5120-8. ⟨10.1021/jf703715j⟩
Europe PubMed Central

مصطلحات موضوعية: Dry-heating, MESH: Hydrogen-Ion Concentration, Time Factors, Food Handling, ph, 030309 nutrition & dietetics, Protein aggregation, food proteins, Whey protein isolate, chemistry.chemical_compound, MESH: Heating, hen egg white lysozyme, [SDV.IDA]Life Sciences [q-bio]/Food engineering, air-water-interface, functional-properties, Food Industry, Organic chemistry, MESH: Animals, Solubility, 0303 health sciences, MESH: Kinetics, biology, Chemistry, MESH: Chickens, ovalbumin, 04 agricultural and veterinary sciences, Hydrogen-Ion Concentration, 040401 food science, MESH: Food Industry, whey-protein isolate, aggregate, [SDV.IDA.SMA]Life Sciences [q-bio]/Food engineering/domain_sdv.ida.sma, Female, foaming properties, Lysozyme, General Agricultural and Biological Sciences, MESH: Food Handling, Egg white, Surface Properties, Foaming agent, Heating, 03 medical and health sciences, 0404 agricultural biotechnology, Adsorption, Animals, surface, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], MESH: Surface Properties, MESH: Time Factors, General Chemistry, MESH: Solubility, Kinetics, Chemical engineering, adsorption, Ionic strength, gelling properties, polysaccharide, MESH: Muramidase, biology.protein, Muramidase, Chickens, MESH: Female

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f066234868f4c516eeeeec586403866Test
https://doi.org/10.1021/jf703715jTest

المؤلفون: Desfougeres, Y., Jardin, Julien, Lechevalier-Datin, Valérie, Pezennec, S., Nau, Francoise

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST

المصدر: ISSN: 1525-7797.

مصطلحات موضوعية: length cross-linking, cyclic-imide, irreversible inactivation, isoaspartate formation, asparaginyl residues, in-vitro, recombinant, antibody, protein-degradation, peptide degradation, alzheimers-disease, MESH: Animals, MESH: Catalysis, MESH: Chickens, MESH: Hot Temperature, MESH: Hydrogen-Ion Concentration, MESH: Muramidase, MESH: Protein Multimerization, MESH: Protein Structure, Tertiary, MESH: Succinimides, MESH: Swine, [SDV.IDA.SMA]Life Sciences [q-bio]/Food engineering/domain_sdv.ida.sma

العلاقة: info:eu-repo/semantics/altIdentifier/pmid/21166442; hal-00729259; https://institut-agro-rennes-angers.hal.science/hal-00729259Test; PRODINRA: 45640; PUBMED: 21166442; WOS: 000285956700021

الإتاحة: https://doi.org/10.1021/bm101089gTest
https://institut-agro-rennes-angers.hal.science/hal-00729259Test

المؤلفون: Salvatore, D.B., Duraffourg, N., Favier, A., Persson, B.A., Lund, M., Delage, M.M., Silvers, R., Schwalbe, H., Croguennec, Thomas, Bouhallab, Said, Forge, V.

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, French National Research Agency, INRA (Rennes, France), CEA (Grenoble, France), Swedish Linneaus Center of Excellence, Polytechnische Stiftung, DEG, state of Hesse

المصدر: ISSN: 1525-7797.

مصطلحات موضوعية: bovine alpha-lactalbumin, molten globule state, egg-white lysozyme, nmr-spectroscopy, phosphotransferase system, beta-lactoglobulin, amyloid, fibrils, metal-ions, binding, aggregation, MESH: Animals, MESH: Cattle, MESH: Muramidase, MESH: Protein Conformation, MESH: Protein Interaction Mapping, MESH: Protein Multimerization, MESH: Static Electricity, MESH: Thermodynamics, MESH: Chickens, MESH: Hydrogen-Ion Concentration, MESH: Hydrophobic and Hydrophilic Interactions, MESH: Kinetics, MESH: Lactalbumin, MESH: Magnetic Resonance Spectroscopy, MESH: Microspheres, MESH: Molecular Dynamics Simulation, [SDV.IDA.SMA]Life Sciences [q-bio]/Food engineering/domain_sdv.ida.sma

العلاقة: info:eu-repo/semantics/altIdentifier/pmid/21545084; hal-00729257; https://institut-agro-rennes-angers.hal.science/hal-00729257Test; PRODINRA: 44646; PUBMED: 21545084; WOS: 000291499900029

الإتاحة: https://doi.org/10.1021/bm200285eTest
https://institut-agro-rennes-angers.hal.science/hal-00729257Test

المؤلفون: Nigen, M., Le Tilly, V., Croguennec, Thomas, Drouin-Kucma, D., Bouhallab, Said

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST

المصدر: ISSN: 0006-3002 ; BBA - Biochimica et Biophysica Acta ; https://institut-agro-rennes-angers.hal.science/hal-00730025Test ; BBA - Biochimica et Biophysica Acta, 2009, 1794 (4), pp.709-15. ⟨10.1016/j.bbapap.2008.12.017⟩.

مصطلحات موضوعية: Fluorescence, compressibility, hydration, proteins, alpha-Lactalbumin, Lysozyme, Interaction, Heterodimer, MESH: Animals, MESH: Apoproteins, MESH: Protein Binding, MESH: Protein Conformation, MESH: Protein Multimerization, MESH: Spectrometry, MESH: Temperature, MESH: Cattle, MESH: Chickens, MESH: Dansyl Compounds, MESH: Fluorescence Polarization, MESH: Kinetics, MESH: Lactalbumin, MESH: Muramidase, MESH: Osmolar Concentration, [SDV.IDA.SMA]Life Sciences [q-bio]/Food engineering/domain_sdv.ida.sma

العلاقة: info:eu-repo/semantics/altIdentifier/pmid/19167527; hal-00730025; https://institut-agro-rennes-angers.hal.science/hal-00730025Test; PRODINRA: 26505; PUBMED: 19167527; WOS: 000264690000016

الإتاحة: https://doi.org/10.1016/j.bbapap.2008.12.017Test
https://institut-agro-rennes-angers.hal.science/hal-00730025Test

المؤلفون: Marie-Madeleine Delage, Thomas Croguennec, Mikael Lund, Harald Schwalbe, Adrien Favier, Vincent Forge, Björn Persson, Robert Silvers, Saïd Bouhallab, Nicolas Duraffourg, Delphine B. Salvatore

المساهمون: Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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]), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Laboratoire de Résonance Magnétique Nucléaire (LRMN), Institut de biologie structurale (IBS - UMR 5075 ), 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)-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), Department of Theoretical Chemistry, Lund University [Lund], Institute for Organic Chemistry and Chemical Biology, Goethe-Universität Frankfurt am Main, French National Research Agency, INRA (Rennes, France), CEA (Grenoble, France), Swedish Linneaus Center of Excellence, Polytechnische Stiftung, DEG, state of Hesse, Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-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), Institut de biologie structurale (IBS - UMR 5075), 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)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

المصدر: Biomacromolecules
Biomacromolecules, American Chemical Society, 2011, 12 (6), pp.2200-2210. ⟨10.1021/bm200285e⟩
Biomacromolecules, American Chemical Society, 2011, 12 (6), pp.2200-10. ⟨10.1021/bm200285e⟩
Biomacromolecules, 2011, 12 (6), pp.2200-2210. ⟨10.1021/bm200285e⟩

مصطلحات موضوعية: fibrils, MESH: Hydrogen-Ion Concentration, Magnetic Resonance Spectroscopy, Polymers and Plastics, Protein Conformation, 01 natural sciences, chemistry.chemical_compound, MESH: Protein Conformation, AMYLOID FIBRILS, Protein Interaction Mapping, BINDING, EGG-WHITE LYSOZYME, Materials Chemistry, Theoretical chemistry, MESH: Animals, MESH: Molecular Dynamics Simulation, MESH: Static Electricity, 0303 health sciences, MESH: Kinetics, Chemistry, MESH: Protein Multimerization, MESH: Hydrophobic and Hydrophilic Interactions, MESH: Chickens, amyloid, Nuclear magnetic resonance spectroscopy, Hydrogen-Ion Concentration, Microspheres, BETA-LACTOGLOBULIN, MESH: Cattle, NMR-SPECTROSCOPY, [SDV.IDA.SMA]Life Sciences [q-bio]/Food engineering/domain_sdv.ida.sma, Thermodynamics, PHOSPHOTRANSFERASE SYSTEM, Lysozyme, MESH: Thermodynamics, Hydrophobic and Hydrophilic Interactions, BOVINE ALPHA-LACTALBUMIN, Static Electricity, Supramolecular chemistry, MESH: Microspheres, Bioengineering, Molecular Dynamics Simulation, 010402 general chemistry, Fibril, Biomaterials, Hydrophobic effect, 03 medical and health sciences, Residue (chemistry), Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, MESH: Magnetic Resonance Spectroscopy, Chemical shift, MESH: Protein Interaction Mapping, AGGREGATION, MESH: Lactalbumin, 0104 chemical sciences, Crystallography, Kinetics, METAL-IONS, MESH: Muramidase, Biophysics, Lactalbumin, Cattle, Muramidase, Protein Multimerization, MOLTEN GLOBULE STATE, Chickens

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cc23ee724678a6d3ed31a2fa8344182Test
https://hal.archives-ouvertes.fr/hal-01137748Test

المؤلفون: Yann Desfougères, Stéphane Pezennec, Françoise Nau, Valérie Lechevalier, Julien Jardin

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

المصدر: Biomacromolecules
Biomacromolecules, American Chemical Society, 2011, 12 (1), pp.156-66. ⟨10.1021/bm101089g⟩
Europe PubMed Central

مصطلحات موضوعية: MESH: Hydrogen-Ion Concentration, Hot Temperature, Polymers and Plastics, Swine, asparaginyl residues, length cross-linking, 01 natural sciences, chemistry.chemical_compound, MESH: Protein Structure, Tertiary, antibody, Materials Chemistry, Organic chemistry, MESH: Animals, recombinant, alzheimers-disease, Deamidation, Imide, MESH: Swine, 0303 health sciences, MESH: Protein Multimerization, MESH: Chickens, Hydrogen-Ion Concentration, Covalent bond, irreversible inactivation, [SDV.IDA.SMA]Life Sciences [q-bio]/Food engineering/domain_sdv.ida.sma, peptide degradation, MESH: Succinimides, Lysozyme, Succinimides, Bioengineering, Protein degradation, in-vitro, MESH: Hot Temperature, 010402 general chemistry, Catalysis, Biomaterials, 03 medical and health sciences, Succinimide, Polymer chemistry, Molecule, Animals, 030304 developmental biology, MESH: Catalysis, Protein tertiary structure, protein-degradation, 0104 chemical sciences, Protein Structure, Tertiary, chemistry, MESH: Muramidase, cyclic-imide, Muramidase, isoaspartate formation, Protein Multimerization, Chickens

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28e6bc612a7e456e2b3e9c71c87f47a3Test
https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00729259Test

المؤلفون: Delphine Drouin-Kucma, Thomas Croguennec, Véronique Le Tilly, Michaël Nigen, Saïd Bouhallab

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Laboratoire d'Ingénierie des Matériaux de Bretagne (LIMATB), Université de Bretagne Sud (UBS)-Université de Brest (UBO)-Institut Brestois du Numérique et des Mathématiques (IBNM), Université de Brest (UBO)-Université de Brest (UBO), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

المصدر: BBA-Biochimica et Biophysica Acta
BBA-Biochimica et Biophysica Acta, Elsevier, 2009, 1794 (4), pp.709-15. ⟨10.1016/j.bbapap.2008.12.017⟩
BBA-Biochimica et Biophysica Acta, Elsevier, 2009, 1794, pp.709-715

مصطلحات موضوعية: Protein Conformation, Biochemistry, Analytical Chemistry, chemistry.chemical_compound, MESH: Apoproteins, Protein structure, MESH: Protein Conformation, MESH: Osmolar Concentration, MESH: Animals, ComputingMilieux_MISCELLANEOUS, Heterodimer, Dansyl Compounds, Lactalbumin, 0303 health sciences, MESH: Kinetics, Chemistry, MESH: Protein Multimerization, 030302 biochemistry & molecular biology, Temperature, MESH: Chickens, Fluorescence, MESH: Temperature, Dissociation constant, MESH: Cattle, compressibility, [SDV.IDA.SMA]Life Sciences [q-bio]/Food engineering/domain_sdv.ida.sma, Lysozyme, hydration, MESH: Spectrometry, Fluorescence, Protein Binding, Interaction, Biophysics, Supramolecular chemistry, Fluorescence Polarization, macromolecular substances, 03 medical and health sciences, Animals, MESH: Protein Binding, Molecular Biology, 030304 developmental biology, alpha-Lactalbumin, MESH: Dansyl Compounds, MESH: Fluorescence Polarization, Osmolar Concentration, proteins, MESH: Lactalbumin, Kinetics, Crystallography, Spectrometry, Fluorescence, Ionic strength, MESH: Muramidase, Cattle, Muramidase, Protein Multimerization, Apoproteins, Chickens, Fluorescence anisotropy

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2a25df8539c812913224eabfe74a77eTest
https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00730025Test