Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Alexander Prodöhl"'
Publikováno v:
Protein Expression and Purification. 56:279-285
Folding and assembly studies with alpha-helical membrane proteins are often hampered by the absence of high-level expression systems as well as by missing suitable in vitro refolding procedures. Experimental constraints and requirements for heterolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce321068f60d889cc5086b0260e846c3
https://doi.org/10.1016/j.pep.2007.08.007
https://doi.org/10.1016/j.pep.2007.08.007
Publikováno v:
Biochimie. 89:1433-1437
Diverse methods have been developed and applied in the recent years to study interaction of transmembrane α-helices and often interaction of single transmembrane helices is followed on SDS-gels. Here we compare two measurements of the stability of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62ae6ff615631f43968aee7cb5012c24
https://doi.org/10.1016/j.biochi.2007.06.006
https://doi.org/10.1016/j.biochi.2007.06.006
Publikováno v:
Current Protein & Peptide Science. 8:45-61
Despite a wide variety of biological functions, alpha-helical membrane proteins display a rather simple transmembrane architecture. Although not many high resolution structures of transmembrane proteins are available today, our understanding of membr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ae9a778d3c0fa11af71254d4b2cd437
https://doi.org/10.2174/138920307779941578
https://doi.org/10.2174/138920307779941578
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1758:1815-1822
Folding, assembly and stability of α-helical membrane proteins is still not very well understood. Several of these membrane proteins contain cofactors, which are essential for their function and which can be involved in protein assembly and/or stabi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b22119a48a19ff60eb7b0aaef8e4045d
https://doi.org/10.1016/j.bbamem.2006.05.009
https://doi.org/10.1016/j.bbamem.2006.05.009
Autor:
Carolin Dreher, Niels Chr. Nielsen, Anna Sigrid Pii Svane, Jarl Underhaug, Daniel E. Otzen, Alexander Prodöhl, Anders Malmendal, Mathias Weber, Christian F. W. Becker, Dirk Schneider
Publikováno v:
Weber, M, Schneider, D, Prodöhl, A, Dreher, C, Becker, C, Underhaug, J, Svane, A S P, Malmendal, A, Nielsen, N C & Otzen, D 2011, ' SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH ', Journal of Molecular Biology, vol. 407, no. 4, pp. 594-606 . https://doi.org/10.1016/j.jmb.2011.02.005
The folding and stabilization of α-helical transmembrane proteins are still not well understood. Following cofactor binding to a membrane protein provides a convenient method to monitor the formation of appropriate native structures. We have analyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cf2d3c0b9a80c08e07578d7cae28848
https://pubmed.ncbi.nlm.nih.gov/21315727
https://pubmed.ncbi.nlm.nih.gov/21315727
Publikováno v:
Journal of bioenergetics and biomembranes. 42(6)
In the genome of the untypical cyanobacterium Gloeobacter violaceus PCC 7421 two potential cytochrome b (6) proteins PetB1 and PetB2 are encoded. Such a situation has not been observed in cyanobacteria, algae and higher plants before, and both protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1895b36cc87e06f843b3b6acb9124cbd
https://pubmed.ncbi.nlm.nih.gov/20237831
https://pubmed.ncbi.nlm.nih.gov/20237831
Publikováno v:
Journal of molecular biology. 382(4)
We have analyzed the role of individual heme-ligating histidine residues for assembly of holo-cytochrome b 6 , and we show that the two hemes b L and b H bind in two subsequent steps to the apo-protein. Binding of the low-potential heme b L is a prer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd2c046b032fd2ded281b162a5881c8a
https://pubmed.ncbi.nlm.nih.gov/18656488
https://pubmed.ncbi.nlm.nih.gov/18656488
Autor:
Thomas Volkmer, Donald M. Engelman, Dirk Schneider, Carmen Finger, Daniel E. Otzen, Alexander Prodöhl
Publikováno v:
Finger, C, Volkmer, A, Prodöhl, A, Otzen, D, Engelman, D M & Schneider, D 2006, ' The stability of transmembrane helix interactions measured in a biological membrane ', Journal of Molecular Biology, vol. 358, no. 5, pp. 1221-1228 .
Finger, C, Volkmer, T, Prohöhl, A, Otzen, D E & Engelman, D M 2006, ' The Stability of Transmembrane Helix Interactions Measured in a Biological Membrane ', Journal of Molecular Biology, vol. 358, pp. 1221-1228 . https://doi.org/10.1016/j.jmb.2006.02.065
Finger, C, Volkmer, T, Prohöhl, A, Otzen, D E & Engelman, D M 2006, ' The Stability of Transmembrane Helix Interactions Measured in a Biological Membrane ', Journal of Molecular Biology, vol. 358, pp. 1221-1228 . https://doi.org/10.1016/j.jmb.2006.02.065
Despite some promising progress in the understanding of membrane protein folding and assembly, there is little experimental information regarding the thermodynamic stability of transmembrane helix interactions and even less on the stability of transm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b77c2d97f49cb56f3b0cc7acd89063a5
https://vbn.aau.dk/da/publications/debe67b0-a626-11db-b8eb-000ea68e967b
https://vbn.aau.dk/da/publications/debe67b0-a626-11db-b8eb-000ea68e967b
Publikováno v:
Journal of molecular biology. 350(4)
To define the structural basis for cofactor binding to membrane proteins, we introduce a manageable model system, which allows us, for the first time, to study the influence of individual transmembrane helices and of single amino acid residues on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f727b481a059536b179dcf076d388677
https://pubmed.ncbi.nlm.nih.gov/15950240
https://pubmed.ncbi.nlm.nih.gov/15950240
Publikováno v:
FEBS Letters. (14):2647-2651
In vivo and in vitro requirements for the formation of cytochrome b(6) were examined to analyze the mechanisms of transmembrane b-type cytochrome formation. After heterologous expression of spinach cytochrome b(6), formation of the holo-cytochrome wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3dc58d3c5bc953c1c3c9a6abc5d5dc82