Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Angeliki Damianoglou"'
Publikováno v:
Biochemistry. 49:2811-2820
Membrane-spanning epidermal growth factor receptor ErbB2 is of key importance in cell division, in which a dimeric complex of the protein is responsible for tyrosine kinase activation following ligand binding. The rat homologue of this receptor (Neu)
Autor:
Alex E. Knight, Suzanne E. Howson, Matthew R. Hicks, Peter Scott, Alison Rodger, Edward J. Crust, Jascindra Ravi, Angeliki Damianoglou
Publikováno v:
Chirality. 20:1029-1038
To obtain accurate and consistent measurements from circular dichroism (CD) instruments over time and from different laboratories, it is important that they are properly calibrated. The characteristics of the available reference materials are not ide
Autor:
Angeliki Damianoglou, Matthew R. Hicks, Paula J. Booth, Jascindra Rajendra, P. Mark Rodger, Alison Rodger
Publikováno v:
Chemical Physics. 326:210-220
The linear dichroism of the visible wavelength transitions of retinal have been used to analyse linear dichroism, spectra to determine the orientation of aromatic and peptide structural motifs of Bacteriorhodopsin incorporated into unilamellar soy be
Autor:
Alison Rodger, John M. Sanderson, Timothy R. Dafforn, Matthew R. Hicks, Catherine J. Pridmore, Jackie A. Mosely, Angeliki Damianoglou
Publikováno v:
Protein & peptide letters, 2010, Vol.17(11), pp.1351-1362
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Here we present data on the kinetics of insertion of melittin, a peptide from bee venom, into lipid membranes of different composition. Another component of bee venom is the enzyme phospholipase A2 (PLA₂). We have examined the interaction of melitt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25021f59c9953388665879d5f6b76320
http://dro.dur.ac.uk/8312/1/8312.pdf
http://dro.dur.ac.uk/8312/1/8312.pdf
Publikováno v:
Journal of molecular biology. 383(2)
Many antibiotic peptides function by binding and inserting into membranes. Understanding this process provides an insight into the fundamentals of both membrane protein folding and antibiotic peptide function. For the first time, in this work, flow-a
Autor:
Timothy R. Dafforn, Angeliki Damianoglou, Alison Rodger, Matthew R. Hicks, Paul Wormell, Søren Vrønning Hoffmann
Publikováno v:
Hicks, M R, Dafforn, T R, Damianoglou, A, Wormell, P, Rodger, A & Hoffmann, S V 2009, ' Synchrotron radiation linear dichroism spectroscopy of the antibiotic peptide gramicidin in lipid membranes ', Analyst, vol. 134, no. 8, pp. 1623-1628 . https://doi.org/10.1039/b902523e
We have developed synchrotron radiation linear dichroism (SRLD) to measure the insertion of peptides into lipid bilayers, significantly improving both signal-to-noise and wavelength range over existing methods. Our wavelength cut-off is currently det