[NMR paper] NMR of paramagnetic metalloproteins in solution: Ubi venire, quo vadis?
NMR of paramagnetic metalloproteins in solution: Ubi venire, quo vadis?
Metalloproteins represent a substantial fraction of the proteome where they have an outsized contribution to enzymology. This stems from the reactivity of transition metals found in the active sites of numerous classes of enzymes that undergo redox and/or spin-state transitions. Notwithstanding, NMR structures of metalloproteins deposited in the PDB are under-represented and NMR studies exploring paramagnetic states are a minute fraction of the overall database content. This state of affairs...
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06-01-2022 11:03 AM
[NMR paper] Paramagnetic effects in NMR for protein structures and ensembles: Studies of metalloproteins
Paramagnetic effects in NMR for protein structures and ensembles: Studies of metalloproteins
Paramagnetic effects on the NMR spectra are known to encode information on structure, electronic properties and dynamics hardly accessible with any other technique, especially in the field of biological systems. Paramagnetism-based restraints are conveniently used for the de novo determination of protein structures, the structural refinement starting from crystallographic models, and for the determination of the internal arrangement of domains with known structures. Conformational variability...
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05-17-2022 10:02 AM
[NMR paper] NMR structures of paramagnetic metalloproteins.
NMR structures of paramagnetic metalloproteins.
Related Articles NMR structures of paramagnetic metalloproteins.
Q Rev Biophys. 2005 May;38(2):167-219
Authors: Arnesano F, Banci L, Piccioli M
Metalloproteins represent a large share of the proteome and many of them contain paramagnetic metal ions. The knowledge, at atomic resolution, of their structure in solution is important to understand processes in which they are involved, such as electron transfer mechanisms, enzymatic reactions, metal homeostasis and metal trafficking, as well as...
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11-25-2010 08:21 PM
[NMR paper] PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion
PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics.
Related Articles PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics.
J Biomol NMR. 1998 Nov;12(4):553-7
Authors: Banci L, Bertini I, Cremonini MA, Gori-Savellini G, Luchinat C, Wüthrich K, Güntert P
The program DYANA, for calculation of solution structures of biomolecules with an algorithm based on simulated annealing by torsion angle dynamics, has been supplemented with a...
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11-17-2010 11:15 PM
[NMR paper] Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigatio
Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
Related Articles Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
J Magn Reson B. 1994 Jul;104(3):230-9
Authors: Bertini I, Jonsson BH, Luchinat C, Pierattelli R, Vila AJ
The title protein with MW 30,000 containing high-spin cobalt (II) has been...
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08-22-2010 03:33 AM
[NMR paper] Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigatio
Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
Related Articles Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
J Magn Reson B. 1994 Jul;104(3):230-9
Authors: Bertini I, Jonsson BH, Luchinat C, Pierattelli R, Vila AJ
The title protein with MW 30,000 containing high-spin cobalt (II) has been...