Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements.
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.
Kresse
H P
HP
Experimentelle Kinderkardiologie, Deutsches Herzzentrum, Lazarettstrasse 36, D-80636 Munich, Germany. kresse@dhm.mhn.de
Czubayko
M
M
Nyakatura
G
G
Vriend
G
G
Sander
C
C
Bloecker
H
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002850:Chromatography, Gel; D004926:Escherichia coli / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D016601:RNA-Binding Proteins / Q000737:chemistry*
D001426:Bacterial Proteins; D010455:Peptides; D016601:RNA-Binding Proteins; C054243:Rop protein, ColE1 plasmid