Metalloproteins represent a large share of the proteomes, with the intrinsic metal ions providing catalytic, regulatory, and structural roles critical to protein functions. Structural characterization of metalloproteins and identification of metal coordination features including numbers and types of ligands and metal-ligand geometry, and mapping the structural and dynamic changes upon metal binding are significant for understanding biological functions of metalloproteins. NMR spectroscopy has long been used as an invaluable tool for structure and dynamic studies of macromolecules. Here we focus on the application of NMR spectroscopy in characterization of metalloproteins, including structural studies and identification of metal coordination spheres by hetero-/homo-nuclear metal NMR spectroscopy. Paramagnetic NMR as well as (13)C directly detected protonless NMR spectroscopy will also be addressed for application to paramagnetic metalloproteins. Moreover, these techniques offer great potential for studies of other non-metal binding macromolecules.
PMID: 21809188 [PubMed - as supplied by publisher]
[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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[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.
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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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[NMR paper] Establishing isostructural metal substitution in metalloproteins using 1H NMR, circul
Establishing isostructural metal substitution in metalloproteins using 1H NMR, circular dichroism, and Fourier transform infrared spectroscopy.
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[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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[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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[NMR paper] Identification of cysteine ligands in metalloproteins using optical and NMR spectrosc
Identification of cysteine ligands in metalloproteins using optical and NMR spectroscopy: cadmium-substituted rubredoxin as a model 2- center.
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Protein...
NMR Studies of Metalloproteins.
Linear Mode
