Enzymatic activation complex formation induced by crowding stress

View at publisher
Authors: Lalita Shahu, Dedunu S. Senarathne, Sandipan Saha, H Peter Lu
Cited by: 0
References: 88

Abstract

. Our results indicate that macromolecules significantly impact the association, dissociation, folding, and unfolding of protein molecules, which may result in several pathways in protein signaling and function in the human body. We have demonstrated that chemical pathways do not solely govern the formation of the CaM-eNOS complex, but that macromolecular crowding also plays a significant role in the formation of an active CaM-eNOS complex. Our results suggest that CaM signaling and NOS functions can be regulated with the combined action of chemical-induced and force-induced pathways, providing new insights into the force-induced pathways for the NOS enzymatic reactions.

Fields of Study & Subjects

Protein Structure and Dynamics Nitric Oxide and Endothelin Effects Protein Kinase Regulation and GTPase Signaling

Publication details

Journal / source
Physical Chemistry Chemical Physics
Volume
28
Issue
8
Pages
5505–5515
Publication date
1 January 2026
Language
EN