Related ArticlesAssignment of active-site protons in the 1H-NMR spectrum of reduced human Cu/Zn superoxide dismutase.
Eur J Biochem. 1991 May 8;197(3):691-7
Authors: Bertini I, Capozzi F, Luchinat C, Piccioli M, Viezzoli MS
600-MHz 1H-NMR and nuclear Overhauser enhancement spectroscopy (NOESY) spectra in 2H2O and H2O, as well as truncated driven NOE difference spectra in H2O of reduced human Cu(II)2Zn(II)2 superoxide dismutase (Cu/Zn SOD) have been recorded and used to assign the active-site proton signals. A derivative with histidines selectively deuteriated in the C2 position has been used for the detection of the HC2 histidine protons, 16 out of 17 observed signals of the 18 active-site histidine ring protons have been assigned. The results are compared with previous proposals based on more limited data sets. The numerous cross peaks confirm that the structure in solution is essentially similar to the crystallographic data obtained on the oxidized form. Probably this holds also for His63 which in the reduced form is not bridging any more the two metal ions. The effects of azide binding on the exchangeable 1H-NMR signals of the reduced protein are also reported.
Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins
Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins
Abstract Biological solid-state nuclear magnetic resonance spectroscopy developed rapidly in the past two decades and emerged as an important tool for structural biology. Resonance assignment is an essential prerequisite for structure determination and the characterization of motional properties of a molecule. Experiments, which rely on carbon or nitrogen detection, suffer, however, from low sensitivity. Recently, we introduced the RAP (Reduced Adjoining Protonation) labeling scheme, which...
nmrlearner
Journal club
0
12-06-2011 08:01 AM
[NMR paper] Exploring the active site of human factor Xa protein by NMR screening of small molecu
Exploring the active site of human factor Xa protein by NMR screening of small molecule probes.
Related Articles Exploring the active site of human factor Xa protein by NMR screening of small molecule probes.
Org Biomol Chem. 2003 Dec 7;1(23):4235-41
Authors: Fielding L, Fletcher D, Rutherford S, Kaur J, Mestres J
A collection of small molecules (MW < 350 Da) was screened for binding to human factor Xa using saturation transfer difference NMR spectroscopy to detect binding. The NMR screening experiments identified four hits. Binding isotherms...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidiz
Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR.
Related Articles Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR.
Biochemistry. 2003 Dec 9;42(48):14139-49
Authors: Trivelli X, Krimm I, Ebel C, Verdoucq L, Prouzet-Mauléon V, Chartier Y, Tsan P, Lauquin G, Meyer Y, Lancelin JM
Peroxiredoxins (Prx's) are a superfamily of thiol-specific antioxidant proteins present in all organisms and involved in the hydroperoxide...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Paramagnetic 1H NMR spectrum of nickel(II) pseudoazurin: investigation of the active
Paramagnetic 1H NMR spectrum of nickel(II) pseudoazurin: investigation of the active site structure and the acid and alkaline transitions.
Related Articles Paramagnetic 1H NMR spectrum of nickel(II) pseudoazurin: investigation of the active site structure and the acid and alkaline transitions.
Inorg Chem. 2002 Dec 16;41(25):6662-72
Authors: Dennison C, Sato K
The paramagnetic (1)H NMR spectrum of Ni(II) pseudoazurin possesses a number of resonances exhibiting sizable Fermi-contact shifts. These have been assigned to protons associated with...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Assignment of the nonexchanging protons of the alpha-spectrin SH3 domain by two- and
Assignment of the nonexchanging protons of the alpha-spectrin SH3 domain by two- and three-dimensional 1H-13C solid-state magic-angle spinning NMR and comparison of solution and solid-state proton chemical shifts.
Related Articles Assignment of the nonexchanging protons of the alpha-spectrin SH3 domain by two- and three-dimensional 1H-13C solid-state magic-angle spinning NMR and comparison of solution and solid-state proton chemical shifts.
Chembiochem. 2001 Dec 3;2(12):906-14
Authors: van Rossum BJ, Castellani F, Rehbein K, Pauli J, Oschkinat H
...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Analysis of stress in the active site of myosin accompanied by conformational changes
Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy.
Related Articles Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy.
Eur J Biochem. 1998 Mar 15;252(3):520-9
Authors: Maruta S, Henry GD, Ohki T, Kambara T, Sykes BD, Ikebe M
Myosin forms stable ternary complexes with ADP and the...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus me
A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin.
Eur J Biochem. 1990 Aug 28;192(1):225-9
Authors: Yamamoto Y, Osawa A, Inoue Y, Chûjô R, Suzuki T
The ferric high-spin form of the myoglobin from the shark Galeorhinus japonicus, which...
Assignment of active-site protons in the 1H-NMR spectrum of reduced human Cu/Zn super
Linear Mode
