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Protein Engineering, Vol. 14, No. 11, 897-901, November 2001
© 2001 Oxford University Press

Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements

Hans P. Kresse1,2, Martin Czubayko3, Gerald Nyakatura4, Gerrit Vriend5, Chris Sander6 and Helmut Bloecker3

1 Experimentelle Kinderkardiologie, Deutsches Herzzentrum, Lazarettstrasse 36, D-80636 Munich, 3 GBF, 38124 Braunschweig, 4 MWG Biotech AG, 85560 Ebersberg, 5 EMBL, 69117 Heidelberg, Germany and 6 EBI, Hinxton, UK

We converted the small homodimeric four-helix bundle repressor of primer protein (Rop) into a monomeric four-helix bundle by introduction of connecting loops. Both left- and right-handed four-helix bundles were produced. The left-handed bundles were more stable and were used to introduce biologically interesting peptides in one of the loops.


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