Zobrazeno 1 - 10 of 11 pro vyhledávání: '"M. R. Egmond"'
1
NMR Studies of Fusarium solani pisi Cutinase in Complex with Phosphonate Inhibitors
Autor: H. M. Verheij, Henri A. M. Pepermans, M. L. M. Mannesse, A. Groenewegen, M. R. Egmond, Cornelis W. Hilbers, Jeanine J. Prompers, B. Van Noorloos
Publikováno v: Biochemistry, 38(19), 5982-5994. American Chemical Society
The backbone dynamics of Fusarium solani pisi cutinase in complex with a phosphonate inhibitor has been studied by a variety of nuclear magnetic resonance experiments to probe internal motions on different time scales. The results have been compared
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01a5d053db0e026ef7ac3b116a8cb6d1
https://doi.org/10.1021/bi990039k
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3
Cloning, expression, purification and characterization of patatin, a novel phospholipase A
Autor: H J, Hirschberg, J W, Simons, N, Dekker, M R, Egmond
Publikováno v: European journal of biochemistry. 268(19)
Patatin is the major protein constituent of potato tubers and displays broad esterase activity. The native enzyme actually belongs to a highly homologous multigene family of vacuolar glycoproteins. From these, the patB2 patatin gene was selected and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9ce643ae3cf48b9793d22e038206e1fe
https://pubmed.ncbi.nlm.nih.gov/11589694
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4
Extraction of peptide tagged cutinase in detergent-based aqueous two-phase systems
Autor: A, Rodenbrock, K, Selber, M R, Egmond, M R, Kula
Publikováno v: Bioseparation. 9(5)
Detergent-based aqueous two-phase systems have the advantage to require only one auxiliary chemical to induce phase separation above the cloud point. In a systematic study the efficiency of tryptophan-rich peptide tags was investigated to enhance the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::29c59ea135450228e1cb4208e6022eb9
https://pubmed.ncbi.nlm.nih.gov/11394565
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5
In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT
Autor: R A, Kramer, D, Zandwijken, M R, Egmond, N, Dekker
Publikováno v: European journal of biochemistry. 267(3)
OmpT is a protease present in the outer membrane of Escherichia coli. The enzyme was overexpressed without its signal sequence in E. coli using a T7 system, resulting in the accumulation of OmpT as inclusion bodies. After solubilization of the inclus
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4a99f7db498b803db464a1b1693663df
https://pubmed.ncbi.nlm.nih.gov/10651827
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8
Engineering surface charges in a subtilisin
Autor: M R, Egmond, W P, Antheunisse, P, Ravestein, A T, Mooren, J, de Vlieg
Publikováno v: Advances in experimental medicine and biology. 379
Introduction of multiple charged amino acid residues in the subtilisin Savinase by genetic engineering allowed us to modify the electrostatic properties of this enzyme in a systematic way. The effects of these charge changes were investigated theoret
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8e084693a98ae5ca9a4104ce0cf1f589
https://pubmed.ncbi.nlm.nih.gov/8796326
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