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1 Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-like transglycosylase
article 2007    
Author: Barends, T.R.M. · Bultema, J.B. · Kaper, T. · Maarel, M.J.E.C. van der · Dijkhuizen, L. · Dijkstra, B.W.
Keywords: Biology · Amylomaltase · Glucans · Glycosyl hydrolases · Conformations · Crystallography · Hydrolysis · Nucleophiles · Oligosaccharides · Polysaccharides · Synthesis (chemical) · Enzyme activity · Food technology · X ray crystallography · alpha-Amylase · Crystallography, X-Ray · Enzyme Stability · Glycogen Debranching Enzyme System · Glycoside Hydrolases · Models, Molecular
[Abstract]

2 Molecular cloning and characterization of the alkaline ceramidase from Pseudomonas aeruginosa PA01
article 2003    
Author: Nieuwenhuizen, W.F. · Leeuwen, S. van · Jack, R.W. · Egmond, M.R. · Götz, F.
Keywords: Biology · Food technology · Ceramidase · Gene · Inclusion body · Pseudomonas · Virulence factor · Amidohydrolases · Amino Acid Sequence · Base Sequence · Cloning, Molecular · Electrophoresis, Agar Gel · Inclusion Bodies · Models, Molecular · Molecular Sequence Data · Pichia · Protein Renaturation · Protein Sorting Signals · Pseudomonas aeruginosa · Recombinant Proteins · Sequence Analysis, Protein · Escherichia coli · Eukaryota · Pichia · Pichia pastoris · Prokaryota · Pseudomonas · Pseudomonas aeruginosa · Pseudomonas putida
[Abstract]

3 Changes at the KinA PAS-A dimerization interface influence histidine kinase function
article 2008    
Author: Lee, J. · Tomchick, D.R. · Brautigam, C.A. · Machius, M. · Kort, R. · Hellingwerf, K.J. · Gardner, K.H.
Keywords: Biology · Bacteria · Catalyst activity · Crystal structure · Dimerization · Bacillus subtilis KinA protein · Histidine kinase function · Proteins · X ray · Amino Acid Sequence · Bacillus subtilis · Bacterial Proteins · Crystallography, X-Ray · Dimerization · Models, Molecular · Molecular Sequence Data · Protein Conformation · Protein Kinases · Bacillus subtilis · Bacteria (microorganisms)
[Abstract]

4 T cells discriminate between differentially phosphorylated forms of αB-crystallin, a major central nervous system myelin antigen
article 1998    
Author: Stipdonk, M.J.B. van · Willems, A.A. · Amor, S. · Persoon-Deen, C. · Travers, P.J. · Boog, C.J.P. · Noort, J.M. van
Keywords: Health · αB-crystallin · Epitope analysis · Heal shock protein · I-A(s) binding motif · Phosphorylation · Post-translational modification · TCR · Amino Acid Sequence · Animals · Binding Sites · Cattle · Computer Simulation · Crystallins · Epitopes · Female · Lymphocyte Activation · Mice · Mice, Inbred Strains · Models, Molecular · Molecular Sequence Data · Phosphorylation · Receptors, Antigen, T-Cell · Serine · T-Lymphocytes
[Abstract]

5 The S-layer protein of Lactobacillus acidophilus ATCC 4356 : identification and characterisation of domains responsible for S-protein assembly and cell wall binding
article 2001    
Author: Smit, E. · Oling, F. · Demel, R. · Martinez, B. · Pouwels, P.H.
Keywords: Biology · Amino Acid Sequence · Bacterial Proteins · Cell Wall · Crystallization · Electrophoresis, Polyacrylamide Gel · Escherichia coli · Lactobacillus acidophilus · Membrane Glycoproteins · Membrane Proteins · Microscopy, Electron · Models, Molecular · Molecular Sequence Data · Peptide Fragments · Phosphatidylserines · Protein Binding · Protein Structure, Quaternary · Protein Structure, Secondary · Protein Structure, Tertiary · Recombinant Fusion Proteins · Sequence Alignment · Sequence Analysis, Protein · Solutions · Trypsin · Escherichia coli · Lactobacillus acidophilus · Lactobacillus casei · Lactobacillus crispatus · Lactobacillus helveticus
[Abstract]

6 Peanut allergen Ara h 1 interacts with proanthocyanidins into higher molecular weight complexes
article 2007    
Author: Boxtel, E.L. van · Broek, L.A.M. van den · Koppelman, S.J. · Vincken, J.-P. · Gruppen, H.
Keywords: Food technology · Ara h 1 · Peanut allergy · Proanthocyanidins · Protein-polyphenol interaction · allergen · Ara h 1 protein, Arachis hypogaea · beta conglycinin protein, Glycine max · beta-conglycinin protein, Glycine max · globulin · glycinin · glycoprotein · proanthocyanidin · soybean protein · vegetable protein · article · chemical structure · chemistry · drug interaction · gel chromatography · ion exchange chromatography · molecular weight · Allergens · Chromatography, Gel · Chromatography, Ion Exchange · Drug Interactions · Globulins · Glycoproteins · Models, Molecular · Molecular Weight · Plant Proteins · Proanthocyanidins · Soybean Proteins · Ara · Arachis hypogaea · Glycine max
[Abstract]

7 Exploring the active center of human acetylcholinesterase with stereomers of an organophosphorus inhibitor with two chiral centers
article 1999    
Author: Ordentlich, A. · Barak, D. · Kronman, C. · Benschop, H.P. · Jong, L.P.A. de · Ariel, N. · Barak, R. · Segall, Y. · Velan, B. · Shafferman, A.
Keywords: Cholinesterase reactivator · Soman · Binding site · Chirality · Dealkylation · Enzyme activity · Enzyme analysis · Enzyme binding · Enzyme specificity · Enzyme structure · Enzyme substrate · Human cell · Protein expression · Stereochemistry · Stereoisomerism · Alkylation · Amino acid substitution · Binding sites · Cell line · Cholinesterase inhibitors · Humans · Hydrogen Bonding · Kidney · Macromolecular substances · Models, Molecular · Mutagenesis, Site-Directed · Stereoisomerism · Acetylcholinesterase, EC 3.1.1.7 · Alanine, 56-41-7 · Phenylalanine, 63-91-2 · Phosphorus, 7723-14-0 · Soman, 96-64-0
[Abstract]

8 Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
article 2003    
Author: Arand, M. · Hallberg, B.M. · Zou, J. · Bergfors, T. · Oesch, F. · Werf, M.J. van der · Bont, J.A.M. de · Jones, T.A. · Mowbray, S.L.
Keywords: Biology · Biotechnology · Crystal structure · Enantioselectivity · Epoxide hydrolase · Mechanism · Monoterpene degradation · bacterial enzyme · limonene 1,2 epoxide hydrolase · selenomethionine · unclassified drug · valpromide · alpha helix · article · beta sheet · catalysis · chemical reaction · crystal structure · detoxification · drug protein binding · enantioselectivity · enzyme active site · enzyme metabolism · enzyme structure · enzyme substrate complex · nonhuman · priority journal · reaction analysis · Rhodococcus erythropolis · site directed mutagenesis · Amino Acid Sequence · Bacterial Proteins · Catalytic Domain · Crystallography, X-Ray · Dimerization · Epoxide Hydrolases · Models, Molecular · Molecular Sequence Data · Mutagenesis, Site-Directed · Protein Subunits · Recombinant Proteins · Rhodococcus · Sequence Homology, Amino Acid · Actinobacteria (class) · Bacteria (microorganisms) · Rhodococcus · Rhodococcus erythropolis · uncultured actinomycete
[Abstract]

9 Molecular characterization of a saline-soluble lectin from a parasitic fungus: Extensive sequence similarities between fungal lectins
article 1996    
Author: Rosén, S. · Kata, M. · Persson, Y. · Lipniunas, P.H. · Wikström, M. · Hondel, C.A.M.J.J. van den · Brink, J.M. van den · Rask, L. · Hedén, L.O. · Tunlid, A.
Keywords: Biology · Electrospray mass spectrometry · Fungal lectin · Primary structure · Secondary structure · Lectin · Amino terminal sequence · Animal cell · Antigenicity · Enzyme specificity · Fungus · Gene disruption · Lectin binding · Mass spectrometry · Molecular recognition · Nonhuman · Priority journal · Protein analysis · Protein processing · Protein protein interaction · Protein secondary structure · Agaricus · Amino Acid Sequence · Antibody Specificity · Base Sequence · Blotting, Southern · Carbohydrate Sequence · Circular Dichroism · Fungal Proteins · Genes, Fungal · Glycosylation · Isoenzymes · Lectins · Mass Spectrometry · Mitosporic Fungi · Models, Molecular · Molecular Sequence Data · Protein Conformation · Protein Structure, Secondary · Sequence Homology, Amino Acid · Sodium Chloride · Solubility · Agaricus bisporus · Animalia · Arthrobotrys · Arthrobotrys oligospora · Basidiomycota · Deuteromycete · Fungi
[Abstract]

10 Properties and applications of starch-converting enzymes of the alpha-amylase family
article 2002    
Author: Maarel, M.J.E.C. van der · Veen, B. van der · Uitdehaag, J.C.M. · Leemhuis, H. · Dijkhuizen, L.
Keywords: Nutrition · α-Amylase · Anti-staling of bread · Glycosylhydrolases · Starch industry · Starch-converting enzymes · Amino acids · Chemical bonds · Conformations · Crystallization · Enzymes · Hydrolysis · Mutagenesis · Substrates · X-ray crystallography · Amylopectin · Cyclodextrin · Cyclomaltodextrin glucanotransferase · Dextrin · Dipeptidyl carboxypeptidase · Fructose · Glucose · Glycosidase · Maltodextrin · Maltose · Maltotriose · Transferase · Bacterium · Crop · Enzyme active site · Enzyme conformation · Enzyme engineering · Enzyme mechanism · Enzyme specificity · Enzyme stability · Enzyme substrate complex · Enzyme synthesis · Food processing · Industrial production · Protein domain · Protein family · Site directed mutagenesis · Structure activity relation · Amino Acid Sequence · Biotechnology · Conserved Sequence · Glycoside Hydrolases · Glycosyltransferases · Models, Molecular · Molecular Sequence Data · Protein Conformation · Sequence Homology, Amino Acid · Substrate Specificity · Manihot esculenta · Solanum tuberosum · Triticum aestivum · Zea mays
[Abstract]

Search results also available in MS Excel format.

Showing 1 to 10 of 10 found. | Sort by date