Zobrazeno 1 - 10
of 100
pro vyhledávání: '"J.M. van der Laan"'
Autor:
Hermand, Jost
Publikováno v:
Monatshefte, 2016 Jul 01. 108(2), 278-279.
Externí odkaz:
http://www.jstor.org/stable/44157173
Autor:
Jost Hermand
Publikováno v:
Monatshefte. 108:278-279
Publikováno v:
Scopus-Elsevier
Proteins-Structure Function and Bioinformatics, 14(2), 178-190. Wiley
Proteins-Structure Function and Bioinformatics, 14(2), 178-190. Wiley
The crystal structure of the reduced form of the enzyme p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, complexed with its substrate p-hydroxybenzoate, has been obtained by protein X-ray crystallography. Crystals of the reduced form were
Autor:
Leonardus Johannes Sofie Marie Mulleners, O. Misset, H. Kelders, A.A. Lammers, Bauke W. Dijkstra, Alexey Teplyakov, J.M. van der Laan, Kor H. Kalk
Publikováno v:
Protein Engineering, 5(5), 413-420
Serine endoproteases such as trypsins and subtilisins are known to have an extended substrate binding region that interacts with residues P6 to P3' of a substrate. In order to investigate the structural and functional effects of replacing residues at
Autor:
D. J. van Schouwen, G. Gerritse, H. N. Scheffers, O. Misset, J.M. van der Laan, Bauke W. Dijkstra, Alexey Teplyakov, Leonardus Johannes Sofie Marie Mulleners
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9780306451089
The ability to remove proteinaceous fabric stains made the alkaline proteases powerful tools in the hands of detergent manufacturers. The application of proteases in detergents requires that the proteases are stable and active in the presence of typi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e0eae7c082745ea2638446ae50a4acfe
https://doi.org/10.1007/978-1-4613-0319-0_22
https://doi.org/10.1007/978-1-4613-0319-0_22
Autor:
O. Misset, Bauke W. Dijkstra, J.M. van der Laan, Leonardus Johannes Sofie Marie Mulleners, H. Kelders, Kor H. Kalk, Alexey Teplyakov
Publikováno v:
Protein Engineering, 5(5), 405-411
The crystal structure of a serine protease from the alkalophilic strain Bacillus alcalophilus PB92 has been determined by X-ray diffraction at 1.75 A resolution. The structure has been solved by molecular replacement using the atomic model of subtili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5f9cc0762923202c6e91f20de4baec2
https://research.rug.nl/en/publications/8b0b8b5d-6970-4fbb-bcc3-6ffb64785e46
https://research.rug.nl/en/publications/8b0b8b5d-6970-4fbb-bcc3-6ffb64785e46
Autor:
J.M. van der Laan-Day
Publikováno v:
Taal en beroep. 19:156-161
The College of Technology student is trained to use technology in practice. In his profession he is society orientated, and his language education should be so too. At this level it is for the first time that languages are no longer an aim in themsel
Autor:
Saraswathula, Anirudh1 (AUTHOR), Porras, Jose L.2 (AUTHOR), Mukherjee, Debraj2 (AUTHOR), Rowan, Nicholas R.1,2 (AUTHOR) nrowan1@jhmi.edu
Publikováno v:
Cancers. Jan2023, Vol. 15 Issue 1, p195. 13p.
Publikováno v:
Biochimica et biophysica acta, 668(2), 268-276
Digestion of β c -hemocyanin yielded tubular polymers as well as so-called collars. Analysis of the collar fraction revealed that it consisted of two fragments, one having a relative molecular mass of approx. 125 000 and the other a relative molecul
Publikováno v:
Journal of Molecular Biology, 165(3), 563-564. Academic Press
The FAD-containing enzyme lipoamide dehydrogenase (EC 1.6.4.3. NADH: lipoamide oxidoreductase) of Azotobacter vinelandii has been crystallized from polyethylene glycol solutions. The space group is P2(1)2(1)2(1) with one dimer in the asymmetric unit.