Zobrazeno 1 - 10 of 17 pro vyhledávání: '"Evamaria I, Petersen"'
1
De novo Design of a Polycarbonate Hydrolase
Autor: Laura H. Holst, Niklas G. Madsen, Freja T. Toftgaard, Freja Roenne, Ioana-Malina Moise, Evamaria I. Petersen, Peter Fojan
Enzymatic degradation of plastics is currently limited to the use of engineered natural enzymes. As of yet, all engineering approaches applied to plastic degrading enzymes retain the natural α/β-fold. While mutations can be used to increase thermos
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::98c3a6896a3a71dd3e17c4df38334bbe
https://doi.org/10.1101/2023.03.10.532063
Zobrazit plný text záznamu
3
EstB from Burkholderia gladioli: A novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activity
Autor: Christoph Kratky, Evamaria I. Petersen, Ulrike Wagner, Helmut Schwab
Publikováno v: Protein Science. 11:467-478
Esterases form a diverse class of enzymes of largely unknown physiological role. Because many drugs and pesticides carry ester functions, the hydrolysis of such compounds forms at least one potential biological function. Carboxylesterases catalyze th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67eb4f7e8501851a1bf0829ea9801e84
https://doi.org/10.1110/ps.33002
Zobrazit plný text záznamu
4
The Interaction of Fusarium solani pisi Cutinase with Long Chain Spin Label Esters
Autor: Kristian Raaby Poulsen, Thomas Kjær Sørensen, Laurent Duroux, Steffen B. Petersen, Evamaria I. Petersen, Reinhard Wimmer
Publikováno v: Aalborg University
Poulsen, K R, Sørensen, T K, Duroux, L, Petersen, E, Petersen, S B & Wimmer, R 2006, ' The interaction of Fusarium solani pisi cutinase with long chain spin label esters ', Biochemistry, vol. 45, no. 30, pp. 9163-9171 .
We here present a study of the interaction between the Fusarium solani pisi cutinase mutant S120A and spin-labeled 4,4-dimethyloxazoline-N-oxyl-(DOXYL)-stearoyl-glycerol substrates in a micellar system. The interaction is detected by NMR measuring ch
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaff072ad582b416f072f4ea1b1dd726
https://doi.org/10.1021/bi060329i
Zobrazit plný text záznamu
5
Engineering the pH-optimum of a triglyceride lipase: from predictions based on electrostatic computations to experimental results
Autor: Maria Teresa Neves-Petersen, Steffen B. Petersen, Rune G. Madsen, Melinda Noronha, Peter Fojan, Evamaria I. Petersen
Publikováno v: Journal of Biotechnology. 87:225-254
The optimisation of enzymes for particular purposes or conditions remains an important target in virtually all protein engineering endeavours. Here, we present a successful strategy for altering the pH-optimum of the triglyceride lipase cutinase from
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae6df5af34daca918f3677340631c2bd
https://doi.org/10.1016/s0168-1656(01)00240-1
Zobrazit plný text záznamu
6
Backbone and sidechain 1H, 13C and 15N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid
Autor: Reinhard Wimmer, Evamaria I. Petersen, Laurent Duroux, Mikka Hansen, Mathilde Jorgensen, Jesper S. Oeemig
Publikováno v: Oeemig, J S, Jørgensen, M L, Hansen, M S, Petersen, E I, Duroux, L, Wimmer, R & Duroux, L 2009, ' Backbone and sidechain 1H, 13C and 15N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid ', Biomolecular NMR Assignments, vol. 3, no. 1, pp. 89-93 . https://doi.org/10.1007/s12104-009-9148-6
In this manuscript, we present the backbone and side chain assignments of human brain-type fatty acid binding protein, also known as FABP7, in its apo form and in four different holo forms, bound to DHA, oleic acid, linoleic acid and elaidic acid.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e2dc1f335a85f68f5eb784310dee532
https://pubmed.ncbi.nlm.nih.gov/19636954
Zobrazit plný text záznamu
7
Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5
Autor: Evamaria I. Petersen, Jacob Dam Sørensen, Marilyn G. Wiebe
Publikováno v: Sørensen, J D, Petersen, E & Wiebe, M G 2007, ' Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5 ', Biotechnology Letters, vol. 29, no. 8, pp. 1227-1232 . https://doi.org/10.1007/s10529-007-9369-7
Sorensen, J D, Petersen, E I & Wiebe, M 2007, ' Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5 ', Biotechnology Letters, vol. 29, no. 8, pp. 1227-1232 . https://doi.org/10.1007/s10529-007-9369-7
Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F. solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bec7c8f23a39d90d2ac9f7f4046c089a
https://vbn.aau.dk/da/publications/322c2630-b544-11dc-a96e-000ea68e967b
Zobrazit plný text záznamu
8
High probability of disrupting a disulphide bridge mediated by an endogenous excited tryptophan residue
Autor: Peter Fojan, Joseph R. Lakowicz, Maria Teresa Neves-Petersen, Steffen B. Petersen, Evamaria I. Petersen, Zygmunt Gryczynski, Shona Pedersen
Publikováno v: Petersen, M T N, Gryczynski, Z, Lakowicz, J, Fojan, P, Pedersen, S, Petersen, E & Petersen, S B 2002, ' High probability of disrupting a disulphide bridge mediated by an endogenous excited tryptophan residue ', Protein Science, vol. 11, pp. 588-600 .
Aalborg University
It is well known that ultraviolet (UV) radiation may reduce or even abolish the biological activity of proteins and enzymes. UV light, as a component of sunlight, is illuminating all light-exposed parts of living organisms, partly composed of protein
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2735e5fd6abe3b1da0320317a50cc161
https://pubmed.ncbi.nlm.nih.gov/11847281
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje