Hofmann, Andreas and Huber, Robert 2003. Liposomes in assessment of annexin–membrane interactions. Methods in Enzymology 372 , pp. 186-216. 10.1016/S0076-6879(03)72011-4 |
Abstract
Annexins show an impressive structural conservation; they share a characteristic topology, calcium-binding sites/membrane loops, and the ability to bind to membrane surfaces. These well-defined properties are contrasted by an enormous variety of possible functions and involvements in physiological pathways. The significant feature of these proteins is the peripheral membrane binding, which is calcium-mediated in the case of the vertebrate members of this protein family. Despite being cytosolic proteins, annexins fulfill their physiological functions in membrane-bound states or by the timed attachment to or desorption from membranes. Annexin–membrane interactions are investigated in the chapter by using liposomes as an object mimicking physiological membranes. Experiments mentioned in the chapter prove that liposomes are a versatile and powerful tool to characterize protein–membrane interactions. To keep track of basic molecular events, liposomes enable a much needed scientific simplification to gain insights into generic mechanisms at the protein–membrane interface.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Biosciences |
Publisher: | Elsevier |
ISSN: | 0076-6879 |
Last Modified: | 24 Jun 2017 11:00 |
URI: | https://orca.cardiff.ac.uk/id/eprint/70175 |
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