This study investigates the multidomain TAZ4 construct of CREB-binding protein (CBP) using NMR spectroscopy. By exploiting differences in relaxation properties, we developed a novel method to distinguish globular domains and intrinsically disordered regions within the same protein. The work enabled detailed sequence-specific assignments, revealed α-helical tendencies in disordered regions, and characterized histidine residues involved in zinc binding. These results offer new insights into the structure and dynamics of multidomain proteins.
Novel methods to investigate multidomain proteins / Silvia Oliveti; Lorenzo Bracaglia; Isabella Caterina Felli; Roberta Pierattelli. - ELETTRONICO. - (2025), pp. 17-17. (Intervento presentato al convegno Division of Chemistry of Biological Systems Italian Chemical Society Conference 2025 tenutosi a University of Trieste nel June 18th-20th 2025).
Novel methods to investigate multidomain proteins
Silvia Oliveti;Lorenzo Bracaglia;Isabella Caterina Felli;Roberta Pierattelli
2025
Abstract
This study investigates the multidomain TAZ4 construct of CREB-binding protein (CBP) using NMR spectroscopy. By exploiting differences in relaxation properties, we developed a novel method to distinguish globular domains and intrinsically disordered regions within the same protein. The work enabled detailed sequence-specific assignments, revealed α-helical tendencies in disordered regions, and characterized histidine residues involved in zinc binding. These results offer new insights into the structure and dynamics of multidomain proteins.
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