This research demonstrates how protein structure affects energy relaxation in blue copper sites, suggesting important implications for metalloprotein functionality.
for azurin. These differences are correlated with variations in structural rigidity and coordination constraints beyond the first coordination spheres of the blue copper site. Our results reveal that, despite conserved metal coordination, the surrounding protein arrangement plays a significant role in shaping ultrafast energy relaxation pathways in metalloprotein.
No takes yet. Share an insight, caveat, or question.
Domenianni et al. (2026) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: