Role of peptide flanking sequences in the binding of AT-hooks to DNA
Department, Center, or Institute
Chemistry
Presentation Format
Poster
Presentation Type
On-campus research
Description
Role of peptide flanking sequences in the binding of AT-hooks to DNAAshleigh Cabanillas, Maddie T., Katelyn Dobbins, Dr. Karen BuchmuellerAT-rich DNA are bound by proteins that contain AT hook motifs, which are defined by a central arginine-glycine-arginine-proline consensus sequence. The Buchmueller lab is investigating the role of the amino acids that flank the RGRP consensus sequence with respect to DNA affinity and local structure of the complex. These changes can be observed and monitored through fluorescence spectroscopy to assess the affinity of the peptides for DNA and circular dichroism (CD) to monitor changes in the global structure of the individual components and the complex. The resultant affinities for a series of peptides ranged from 0.03 mM to 0.16 mM. However, most peptides had comparable affinities around 0.07 mM, indicating that certain changes in flanking sequences resulted in only minimal changes in affinity.
Session Number
5
Start Date and Time
4-9-2019 4:00 PM
Location
PAC Gym
Recommended Citation
Cabanillas, Ashleigh, "Role of peptide flanking sequences in the binding of AT-hooks to DNA" (2019). Furman Engaged!. 370.
https://scholarexchange.furman.edu/furmanengaged/2019/all/370
Role of peptide flanking sequences in the binding of AT-hooks to DNA
PAC Gym
Role of peptide flanking sequences in the binding of AT-hooks to DNAAshleigh Cabanillas, Maddie T., Katelyn Dobbins, Dr. Karen BuchmuellerAT-rich DNA are bound by proteins that contain AT hook motifs, which are defined by a central arginine-glycine-arginine-proline consensus sequence. The Buchmueller lab is investigating the role of the amino acids that flank the RGRP consensus sequence with respect to DNA affinity and local structure of the complex. These changes can be observed and monitored through fluorescence spectroscopy to assess the affinity of the peptides for DNA and circular dichroism (CD) to monitor changes in the global structure of the individual components and the complex. The resultant affinities for a series of peptides ranged from 0.03 mM to 0.16 mM. However, most peptides had comparable affinities around 0.07 mM, indicating that certain changes in flanking sequences resulted in only minimal changes in affinity.