1. References

Rop (also known as repressor of primer) is a small protein responsible for keeping the copy number of ColE1 and related bacterial plasmids low in E. coli. Structurally, Rop is a homodimeric four-helix bundle protein formed by the antiparallel interaction of two helix-turn-helix monomers. The Rop protein's structure has been solved to high resolution.{{ref|Banner}} Due to its small size and known structure, Rop has been used in protein design work to rearrange its helical topology and reengineer its loop regions.{{ref|Kresse}} In general, the four-helix bundle has been extensively used in de novo protein design work as a simple model to understand the relationship between amino acid sequence and structure.

References

1. {{note|Banner}} {{cite journal|last1=Banner|first1=David W.|last2=Kokkinidis|first2=Michael|last3=Tsernoglou|first3=Demetrius|title=Structure of the ColE1 Rop protein at 1.7 Å resolution|journal=Journal of Molecular Biology|date=August 1987|volume=196|issue=3|pages=657–675|doi=10.1016/0022-2836(87)90039-8|pmid=3681971}}

1. {{note|Kresse}} {{cite journal|last1=Kresse|first1=H. P.|last2=Czubayko|first2=M.|last3=Nyakatura|first3=G.|last4=Vriend|first4=G.|last5=Sander|first5=C.|last6=Bloecker|first6=H.|title=Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements|journal=Protein Engineering Design and Selection|date=1 November 2001|volume=14|issue=11|pages=897–901|doi=10.1093/protein/14.11.897|pmid=11742109}}

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