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المصدر: Journal of Agricultural and Food Chemistry, 21, 55, 8772-8778
Journal of Agricultural and Food Chemistry, 55(21), 8772-8778
Journal of Agricultural and Food Chemistry 55 (2007) 21

مصطلحات موضوعية: glycoprotein, Models, Molecular, Glycine max, major proteins, glycinin, Trimer, soybean protein, cupin superfamily, soybean seeds, Legumin, Drug Interactions, vegetable protein, proanthocyanidin, Soy protein, Plant Proteins, degradation, chemistry.chemical_classification, mechanisms, Ara, biology, Food Chemistry, Seed Storage Proteins, article, food and beverages, Ara h 1 protein, Arachis hypogaea, ion exchange chromatography, Chromatography, Ion Exchange, Biochemistry, Proanthocyanidin, Chromatography, Gel, Soybean Proteins, Protein-polyphenol interaction, lipids (amino acids, peptides, and proteins), General Agricultural and Biological Sciences, h-i, allergen, beta-conglycinin, Peanut allergy, Globulin, gel chromatography, Chemical structure, chemistry, globulin, Food technology, Arachis hypogaea, BBP Sustainable Chemistry & Technology, Ara h 1, Levensmiddelenchemie, Proanthocyanidins, Glycoproteins, VLAG, drug interaction, protein complexes, Molecular mass, ige-binding, Membrane Proteins, molecular weight, Globulins, General Chemistry, Antigens, Plant, Allergens, biochemical phenomena, metabolism, and nutrition, carbohydrates (lipids), chemical structure, biology.protein, Glycoprotein, beta conglycinin protein, Glycine max, beta-conglycinin protein, Glycine max

وصف الملف: application/octet-stream; application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77c0a00c8600db3a3f451f841b345568Test
https://doi.org/10.1021/jf071585kTest

6

The structures of inhibitor complexes of Pyrococcus furiosus Phosphoglucose Isomerase provide insights into substrate binding and catalysis

المؤلفون: G. Michael Blackburn, John M. Berrisford, Renaud Hardré, Svetlana E. Sedelnikova, Jasper Akerboom, Andrew P. Turnbull, Laurent Salmon, Iain A. Murray, John van der Oost, Patrick J. Baker, Stan J. J. Brouns, David W. Rice

المصدر: Journal of Molecular Biology, 343(3), 649-657
Journal of Molecular Biology 343 (2004) 3

مصطلحات موضوعية: Models, Molecular, Glucose-6-phosphate isomerase, Stereochemistry, Protein Conformation, 5-phospho-d-arabinonohydroxamic acid, Archaeal Proteins, rabbit, Glucose-6-Phosphate, mechanism, Isomerase, Crystallography, X-Ray, cupin superfamily, Microbiology, Catalysis, autocrine motility factor, Structural Biology, Microbiologie, angstrom resolution, Molecular replacement, Molecular Biology, VLAG, chemistry.chemical_classification, Manganese, Pentosephosphates, Binding Sites, biology, Molecular Structure, Fructosephosphates, Glucose-6-Phosphate Isomerase, Active site, crystal-structure, Glutamic acid, biology.organism_classification, glycolytic enzyme, molecular replacement, Pyrococcus furiosus, Enzyme, chemistry, Biochemistry, Enzyme inhibitor, biology.protein, protein, Dimerization, Protein Binding

وصف الملف: application/octet-stream; application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6342825034c3b1d7528fe4e0b3437d4Test
https://doi.org/10.1016/j.jmb.2004.08.061Test

7

Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus

المؤلفون: Roberto A. Steiner, Tjaard Pijning, Henriëtte J. Rozeboom, Kor H. Kalk, Fabrizia Fusetti, Maarten R. Egmond, Paula I. van Noort, Klaus H Schröter, Bauke W Dijkstra

المساهمون: Groningen Biomolecular Sciences and Biotechnology, Enzymology, X-ray Crystallography, Membraan enzymologie, Universiteit Utrecht, Dep Scheikunde

المصدر: Structure, 10(2), 259-268. CELL PRESS

مصطلحات موضوعية: Models, Molecular, glycoprotein, Glycosylation, Stereochemistry, Dimer, X-RAYS, Molecular Sequence Data, Static Electricity, MODELS, chemistry.chemical_element, ANGSTROM RESOLUTION, Crystal structure, Crystallography, X-Ray, Copper, Cupin, Dioxygenase, Glycoprotein, Quercetin, X-ray structure, Dioxygenases, Substrate Specificity, quercetin, chemistry.chemical_compound, DIFFRACTION DATA, Structural Biology, Oxidoreductase, Amino Acid Sequence, Protein Structure, Quaternary, Molecular Biology, SEED STORAGE PROTEINS, chemistry.chemical_classification, Binding Sites, cupin, biology, Active site, FLAVONOL, Protein Structure, Tertiary, Trigonal bipyramidal molecular geometry, Aspergillus, chemistry, Docking (molecular), copper, DIOXYGENASE, Oxygenases, biology.protein, Sequence Alignment, BOND

وصف الملف: application/pdf; image/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b7fd17442d1777e842562de802a8480Test
https://research.rug.nl/en/publications/35f581ad-bea7-4dab-97d9-b05187cb9e33Test

8

Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: A special subgroup of the type III extradiol dioxygenases

المؤلفون: Hui Rong, Liwen Niu, Deqiang Wang, Wenying Tang, Maikun Teng, Min Guo, Qun Liu, Quan Hao, Jun Fan, Honghua Ge, Xiaowu Li

مصطلحات موضوعية: Models, Molecular, 2-His-1-carboxylate facial triad, Stereochemistry, Protein Conformation, Saccharomyces cerevisiae, Molecular Sequence Data, Sequence alignment, Crystallography, X-Ray, Biochemistry, Catalysis, Substrate Specificity, Protein structure, Dioxygenase, Animals, Humans, 3-Hydroxyanthranilate 3,4-Dioxygenase, Amino Acid Sequence, Binding site, Kynurenine pathway, Molecular Biology, Peptide sequence, Extradiol dioxygenase, X-ray crystallography, Cupin superfamily, Binding Sites, biology, MAD, Active site, Articles, biology.organism_classification, 3-hydroxyanthranilic acid 3,4-dioxygenase, biology.protein, Oxygenases, NAD+ kinase, Crystallization, Dimerization, Sequence Alignment

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68d6e0c7cb06e963512fa91f2034f277Test
https://europepmc.org/articles/PMC2242480Test/

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