Modularly assembled Zinc Finger Proteins (ZFPs) have been created to recognize a majority of three base pair target sites, yet, gaps exist in their ability to recognize 5’-TNN-3’ target sites. Utilizing the Homeodomain’s ability to bind thiamine and adenine rich sequences in combination with ZFPs, these recognition gaps can be resolved. Here, the composition of an inter-domain linker between a Homeodomain and a two finger ZFP was optimized to create chimeras that bind with high affinity and specificity.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Pankratov, Alexander K.

Contributors

• Wolfe, Scot

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042513-153649

Advisor

• Heilman, Destin

Year

• 2013

Sponsor

• University of Massachusetts Medical School

Date created

• 2013-04-25

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright