The Role of Protein Electrostatics in Facilitating the Catalysis of DEAD-box Proteins
Christopher M. Frenz

TL;DR
This paper explores how electrostatic states in DEAD-box proteins influence their catalytic activity, showing that ligand-induced structural changes modulate electrostatics to facilitate catalysis.
Contribution
It reveals the conserved electrostatic features in DEAD-box motifs and demonstrates how ligand binding alters electrostatics to enhance catalysis.
Findings
Electrostatic states are conserved among DEAD-box motifs.
Ligand binding induces structural changes that modify electrostatics.
Altered electrostatics facilitate the catalytic role of DEAD-box glutamate.
Abstract
Protein electrostatic states have been demonstrated to play crucial roles in catalysis, ligand binding, protein stability, and in the modulation of allosteric effects. Electrostatic states are demonstrated to appear conserved among DEAD-box motifs and evidence is presented that the structural changes that occur to DEAD box proteins upon ligand binding alter the DEAD-box motif electrostatics in a way the facilitates the catalytic role of the DEAD-box glutatmate.
Peer Reviews
No public reviews on file for this paper yet. If you reviewed it on a platform where reviews are public (OpenReview, ICLR, NeurIPS, ICML), you can paste yours below so the community can read it here.
Videos
No videos yet. Explain this paper in a talk, walkthrough, or lecture? Add one.
Taxonomy
TopicsProtein Structure and Dynamics · Enzyme Structure and Function · Endoplasmic Reticulum Stress and Disease
