Major
Chemistry
Anticipated Graduation Year
2025
Access Type
Restricted Access
Abstract
Lanthanides (Ln3+) are of significant importance given their crucial role in modern technology and medicine. However, the process of extracting, isolating, and purifying these elements is prone to challenges. Lanmodulin (LanM), a novel Ln3+-binding protein is capable of selective Ln3+ binding through its EF-hand motifs.1-2 This selectivity is largely attributed to acidic residues in the EF-hand loop. Herein, we present molecular insights into the effect of varying negative charges in a prototypical EF-hand motif on its binding affinity to La³⁺, where the obtained insights could be helpful for future molecular designs of various purposes.
Faculty Mentors & Instructors
Bailey Hanson, Madelyn Smith, Pengfei Li
Creative Commons License

This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Influence of Residue Charge on Peptide Structure and Metal Ion Binding in EF-Hand Motifs
Lanthanides (Ln3+) are of significant importance given their crucial role in modern technology and medicine. However, the process of extracting, isolating, and purifying these elements is prone to challenges. Lanmodulin (LanM), a novel Ln3+-binding protein is capable of selective Ln3+ binding through its EF-hand motifs.1-2 This selectivity is largely attributed to acidic residues in the EF-hand loop. Herein, we present molecular insights into the effect of varying negative charges in a prototypical EF-hand motif on its binding affinity to La³⁺, where the obtained insights could be helpful for future molecular designs of various purposes.