In this issue of Structure, Besaw et al.1 report a well-designed study combining electron paramagnetic resonance measurements and structural analyses of di-histidine-Cu(II)-nitrilotriacetate binding sites in T4 lysozyme. The gained insights could have broad implications for the use of double electron-electron resonance spectroscopy in the elucidation of subtle protein conformational variations.
Di-His-Cu(II)-NTA spin labels for probing protein dynamics: Support from a combined crystallographic/EPR study / Ferraro, Giarita; Garribba, Eugenio; Merlino, Antonello. - In: STRUCTURE. - ISSN 0969-2126. - 34:4(2026), pp. 547-549. [10.1016/j.str.2026.02.016]
Di-His-Cu(II)-NTA spin labels for probing protein dynamics: Support from a combined crystallographic/EPR study
Ferraro, Giarita;Merlino, Antonello
2026
Abstract
In this issue of Structure, Besaw et al.1 report a well-designed study combining electron paramagnetic resonance measurements and structural analyses of di-histidine-Cu(II)-nitrilotriacetate binding sites in T4 lysozyme. The gained insights could have broad implications for the use of double electron-electron resonance spectroscopy in the elucidation of subtle protein conformational variations.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
