Searched for: subject%3A%22Protein%255C%252BBinding%22
(1 - 6 of 6)
document
TNO Kwaliteit van Leven (author), van der Horst, M.A. (author), Arents, J.C. (author), Kort, R. (author), Hellingwerf, K.J. (author)
The bacterial photoreceptor protein photoactive yellow protein (PYP) covalently binds the chromophore 4-hydroxy coumaric acid, tuning (spectral) characteristics of this cofactor. Here, we study this binding and tuning using a combination of pointmutations and chromophore analogs. In all photosensor proteins studied to date the covalent linkage...
article 2007
document
Joosten, V. (author), Roelofs, M.S. (author), van den Dries, N. (author), Goosen, T. (author), Verrips, C.T. (author), van den Hondel, C.A.M.J.J. (author), Lokman, B.C. (author), TNO Kwaliteit van Leven (author)
The Arthromyces ramosus peroxidase gene (arp) was genetically fused to either the 5′- or 3′-terminal ends of the gene encoding llama variable heavy chain antibody fragment VHH R9, resulting in the fusion expression cassettes ARP-R9 or R9-ARP. Aspergillus awamori transformants were obtained which produced up to 30 mg l-1 fusion protein in the...
article 2005
document
Broersen, K. (author), Voragen, A.G.J. (author), Hamer, R.J. (author), de Jongh, H.H.J. (author), TNO Voeding (author)
In this article we show how various degrees of glycosylation can be used to control the thermal stability of proteins. The primary amines of β-lactoglobulin were glycosylated with glucose or fructose within a range of non-denaturing reaction parameters. The modified fractions were characterized and analyzed for structural stability and...
article 2004
document
Nieuwenhuizen, W.F. (author), Dekker, H.L. (author), Gröneveld, T. (author), de Koster, C.G. (author), de Jong, G.A.H. (author), TNO Voeding (author)
Bovine β-lactoglobulin (BLG) is a major component in whey and its physical properties are important for the texture of many dairy-based foods. Modification of proteins with transglutaminase from Streptoverticillium mobaraense (MTGase) can be used to alter their physical properties. MTGase-mediated modification of native BLG was until now,...
article 2004
document
Kosters, H.A. (author), Broersen, K. (author), de Groot, J. (author), Simons, J.W.F.A. (author), Wierenga, P. (author), de Jongh, H.H.J. (author), TNO Voeding (author)
Processing of ovalbumin may result in proteins that differ more than 23°C in denaturation temperature while the structural fold is not significantly affected. This is achieved by 1) conversion of positive residues into negative ones (succinylation); 2) elimination of negative charges (methylation); 3) reducing the proteins hydrophobic exposure ...
article 2003
document
Arand, M. (author), Hallberg, B.M. (author), Zou, J. (author), Bergfors, T. (author), Oesch, F. (author), van der Werf, M.J. (author), de Bont, J.A.M. (author), Jones, T.A. (author), Mowbray, S.L. (author)
Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an α/β hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus...
article 2003
Searched for: subject%3A%22Protein%255C%252BBinding%22
(1 - 6 of 6)