Folding studies on a model b-meander: the D1 domain of a copper amine

Neil Ferguson, 7 Hyde Park Terrace, Leeds,W. Yorkshire,England.LS6 1BJ

A focus of considerable scientific interest is in the area of protein
folding. However much contemporary research has been performed using
predominantly alpha-helical model protein systems. In an attempt to
gain complementary information on folding pathways I am attempting to
establish alternative (b-sheet) model folding systems. Recently the
crystal structure of the E. coli copper amine oxidase has been solved
to high resolution, revealing the presence of an N-terminal b-sheet
domain with few intramolecular contacts to the main body of the
protein. This gene encoding this domain has been subcloned and
expressed and a purification strategy is currently being implemented.
It is hoped that by April preliminary CD/fluorescence spectroscopy
work will have determined the reversibility of folding of this
recombinant protein module and thus its utility as a model folding
system.If successful the structure will be solved by NMR before
further studies.It is anticipated that (in parallel) other classes of
b-sheet protein will be similarly investigated (e.g. b-barrel and
jellyroll motifs).

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