Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Jelle B. Bultema"'
Publikováno v:
FEBS Open Bio, Vol 4, Iss C, Pp 1015-1020 (2014)
The Bacillus circulans ATCC 31382 β-galactosidase (BgaD) is a retaining-type glycosidase of glycoside hydrolase family 2 (GH2). Its commercial enzyme preparation, Biolacta N5, is used for commercial-scale production of galacto-oligosaccharides (GOS)
Externí odkaz:
https://doaj.org/article/88f68fd6b94d4e2a9890a76f0e48f621
Publikováno v:
Food Chemistry, 225:j.foodchem.2017.01.030, 230-238. ELSEVIER SCI LTD
β-Galactosidase enzymes are used in the dairy industry to convert lactose into galactooligosaccharides (GOS) that are added to infant formula to mimic the molecular sizes and prebiotic functions of human milk oligosaccharides. Here we report a detai
Autor:
Siva Krishna Mohan Nalluri, Bart Jan Ravoo, Jelle B. Bultema, Jens Voskuhl, Egbert J. Boekema
Publikováno v:
Angewandte Chemie-International Edition, 50(41), 9747-9751. WILEY-V C H VERLAG GMBH
The wavelength determines whether DNA is captured in a light-responsive ternary supramolecular complex or released (see scheme). The reversible binding of DNA is triggered by a photoisomerization, which switches the complex from a multivalent to a mo
Autor:
Bart Jan Ravoo, Egbert J. Boekema, Jelle B. Bultema, Jens Voskuhl, Siva Krishna Mohan Nalluri
Publikováno v:
Angewandte Chemie. 123:9921-9925
Autor:
Marieke R Beijer, Mark J. Dickman, Edze R. Westra, Kaihong Zhou, Sakharam P Waghmare, Rolf Wagner, Reinhild Wurm, Jennifer A. Doudna, Egbert J. Boekema, Stan J. J. Brouns, Magnus Lundgren, Blake Wiedenheft, Ümit Pul, Matthijs M. Jore, Esther van Duijn, Albert J. R. Heck, Arjan Barendregt, Ambrosius P. Snijders, Jelle B. Bultema, John van der Oost
Publikováno v:
Nature Structural and Molecular Biology 18 (2011) 5
Nature Structural and Molecular Biology, 18(5), 529-536
Nature Structural & Molecular Biology, 18(5), 529-U141. Nature Publishing Group
Nature Structural and Molecular Biology, 18(5), 529-536
Nature Structural & Molecular Biology, 18(5), 529-U141. Nature Publishing Group
The CRISPR (clustered regularly interspaced short palindromic repeats) immune system in prokaryotes uses small guide RNAs to neutralize invading viruses and plasmids. In Escherichia coli, immunity depends on a ribonucleoprotein complex called Cascade
Autor:
Roman Kouřil, Iosifina Sarrou, Petra Fromme, Rajagopal Subramanyam, Craig Jolley, Jelle B. Bultema, Egbert J. Boekema, Jason Greyslak, Balakumar Thangaraj, Su Lin, Julian P. Whitelegge
Publikováno v:
Biophysical Journal, 100(1), 135-143. CELL PRESS
Photosystem I-light harvesting complex I (PSI-LHCI) was isolated from the thermoacidophilic red alga Galdieria sulphuraria, and its structure, composition, and light-harvesting function were characterized by electron microscopy, mass spectrometry, an
Publikováno v:
FEBS Letters. 584:2510-2515
Ongoing progress in electron microscopy (EM) offers now an opening to visualize cells at the nanoscale by cryo-electron tomography (ET). Large protein complexes can be resolved at near-atomic resolution by single particle averaging. Some examples fro
Publikováno v:
Biochimica et Biophysica Acta, 1787(1), 60-67
The individual protein complexes of the oxidative phosphorylation system (OXPHOS complexes 1 to V) specifically interact and form defined supramolecular structures, the so-called "respiratory supercomplexes". Some supercomplexes appear to associate i
Autor:
Jelle B. Bultema, Thomas R. M. Barends, Marc J. E. C. van der Maarel, Lubbert Dijkhuizen, Thijs Kaper, Bauke W. Dijkstra
Publikováno v:
The Journal of Biological Chemistry, 282(23), 17242-17249. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Amylomaltases are glycosyl hydrolases belonging to glycoside hydrolase family 77 that are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides. Using protein crystallography, we have generated a flip book mo
Autor:
Jaap Broos, Eric R. Geertsma, Berend Poolman, Elisa B. Vervoort, Jelle B. Bultema, Gea K. Schuurman-Wolters
Publikováno v:
Journal of Molecular Biology, 346(3), 733-743. Academic Press
The mannitol permease (EII(Mtl)) from Escherichia coli couples mannitol transport to phosphorylation of the substrate. Renewed topology prediction of the membrane-embedded C domain suggested that EII(Mtl) contains more membrane-embedded segments than