Related ArticlesEstablishing isostructural metal substitution in metalloproteins using 1H NMR, circular dichroism, and Fourier transform infrared spectroscopy.
Protein Sci. 1995 Aug;4(8):1571-6
Authors: Pountney DL, Henehan CJ, Vasák M
Far-UV CD, 1H-NMR, and Fourier transform infrared (FTIR) spectroscopy are three of the most commonly used methods for the determination of protein secondary structure composition. These methods are compared and evaluated as a means of establishing isostructural metal substitution in metalloproteins, using the crystallographically defined rubredoxin from Desulfovibrio gigas and its well-characterized cadmium derivative as a model system. It is concluded that analysis of the FTIR spectrum of the protein amide I resonance represents the most facile and generally applicable method of determining whether the overall structure of a metalloprotein has been altered upon metal reconstitution. This technique requires relatively little biological material (ca. 300 micrograms total protein) and, unlike either CD or 1H-NMR spectroscopy, is unaffected by the presence of different metal ions, thus allowing the direct comparison of FTIR spectra before and after metal substitution.
Probing Transient HoogsteenHydrogen Bonds in CanonicalDuplex DNA Using NMR Relaxation Dispersion and Single-Atom Substitution
Probing Transient HoogsteenHydrogen Bonds in CanonicalDuplex DNA Using NMR Relaxation Dispersion and Single-Atom Substitution
Evgenia N. Nikolova, Federico L. Gottardo and Hashim M. Al-Hashimi
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2117816/aop/images/medium/ja-2011-117816_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2117816
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Solution NMR Approaches for Establishing Specificity of Weak Heterodimerization of Membrane Proteins
Solution NMR Approaches for Establishing Specificity of Weak Heterodimerization of Membrane Proteins
Tiandi Zhuang, Bing K. Jap and Charles R. Sanders
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja208972h/aop/images/medium/ja-2011-08972h_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja208972h
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NMR Studies of Metalloproteins.
NMR Studies of Metalloproteins.
NMR Studies of Metalloproteins.
Top Curr Chem. 2011 Aug 2;
Authors: Li H, Sun H
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...
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[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.
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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[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.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Identification of cysteine ligands in metalloproteins using optical and NMR spectroscopy: cadmium-substituted rubredoxin as a model 2- center.
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Establishing isostructural metal substitution in metalloproteins using 1H NMR, circul
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