Almost half of all known enzymes are metalloproteins where themetal center(s) are essential for catalysis, electron transfer, metalstorage/transport, or provide stability and structural properties.NMR is a privileged method for characterizing metalloproteinsproviding the structure at atomic resolution, information aboutamplitude and time-scale of internal dynamics, hints on elec-tronic structure and oxidation states in conditions that mimic thephysiological context. However, in a significant part of the metal-loproteome the metal ion is paramagnetic and, in its vicinity, a“blind sphere” exists where nuclear relaxation is enhanced andsignal detection becomes a challenge

Abolishing "structural blindness" in metalloproteins: PioC, a NOE-less protein structure / Trindade, IB; Invernici, M; Cantini, F; Piccioli, M; Louro, RO. - In: FEBS OPENBIO. - ISSN 2211-5463. - ELETTRONICO. - 11:(2021), pp. 23-23. [10.1002/2211-5463.13234]

Abolishing "structural blindness" in metalloproteins: PioC, a NOE-less protein structure

Invernici, M;Cantini, F;Piccioli, M;
2021

Abstract

Almost half of all known enzymes are metalloproteins where themetal center(s) are essential for catalysis, electron transfer, metalstorage/transport, or provide stability and structural properties.NMR is a privileged method for characterizing metalloproteinsproviding the structure at atomic resolution, information aboutamplitude and time-scale of internal dynamics, hints on elec-tronic structure and oxidation states in conditions that mimic thephysiological context. However, in a significant part of the metal-loproteome the metal ion is paramagnetic and, in its vicinity, a“blind sphere” exists where nuclear relaxation is enhanced andsignal detection becomes a challenge
2021
11
23
23
Goal 4: Quality education
Trindade, IB; Invernici, M; Cantini, F; Piccioli, M; Louro, RO
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1294949
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? 0
social impact