Investigating the Mechanism of cis Amide Bond Stabilization in Phosphoserine‐Proline Sequences
Abstract
Phosphorylation is a reversible covalent modification to biomolecules that is central to protein‐protein interactions, signal transduction, and gene expression. When improperly regulated, phosphorylation can trigger oncogenesis and neurodegenerative diseases such as Alzheimer's disease (AD) and chronic traumatic encephalopathy (CTE). Phosphorylation can also act as a structural switch for cis‐trans isomerization of peptide bonds: through intraresidue phosphate‐amide hydrogen bonds, phosphorylated residues promote compact trans conformations. In other contexts, phosphorylated Serine (pSer) residues can promote cis peptide bonds through unknown mechanisms. To investigate the basis for these structural effects, a series of X‐pSer‐Pro‐Z peptides was synthesized with modifications on the proline, N‐terminal to pSer (X), and C‐terminal to Pro (Z).
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Apr 01, 2018
- Source ID
- 10.1096/fasebj.2018.32.1_supplement.794.9
Entities
People
- Himal K. Ganguly
- Neal J Zondlo
- Nicole R. Raniszewski
Organizations
- United States Department of Defense
- University of Delaware