Related Articles1H NMR resonance assignments in a paramagnetic heme protein by two-dimensional spectroscopy: heme resonances in equine met-azido myoglobin.
Biochem Biophys Res Commun. 1991 Mar 15;175(2):515-9
Authors: Peyton DH
Specific heme protons for the majority of resonances in the downfield resolved region of equine met-azido myoglobin have been assigned using solely the two-dimensional 1H NMR experiments NOESY and COSY. Metazido myoglobin provides a useful test case for the applicability of these techniques to paramagnetic proteins for the following reasons. First met-azido myoglobin is a mixed spin-state protein, with significantly shorter relaxation times and broadened lines relative to pure low-spin systems (eg., met-cyano myoglobin). Second, met-azido hemoglobin and met-azido myoglobin are important as models for the physiological forms of hemoglobin. Third, a few sperm whale met-azido myoglobin resonances have been previously assigned, which permits a comparison of assignments for these similar proteins, and a check of the method presented here.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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[NMR paper] Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Related Articles Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
J Biol Chem. 2003 Mar 7;278(10):7765-74
Authors: Wang X, Tachikawa H, Yi X, Manoj KM, Hager LP
The heme active site structure of chloroperoxidase (CPO), a glycoprotein that displays versatile catalytic activities isolated from the marine mold Caldariomyces fumago, has been characterized by two-dimensional NMR spectroscopic studies. All hyperfine shifted resonances...
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[NMR paper] Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectr
Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.
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 Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.
Eur J Biochem. 1994 Feb 1;219(3):887-96
Authors: Orekhov VYu , Pervushin KV, Arseniev AS
The backbone dynamics of a uniformly 15N-labelled proteolytic fragment (residues 1-71) of bacteriorhodopsin,...
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[NMR paper] Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectr
Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.
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 Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.
Eur J Biochem. 1994 Feb 1;219(3):887-96
Authors: Orekhov VYu , Pervushin KV, Arseniev AS
The backbone dynamics of a uniformly 15N-labelled proteolytic fragment (residues 1-71) of bacteriorhodopsin,...
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[NMR paper] Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Related Articles Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Biochemistry. 1994 Sep 13;33(36):10934-43
Authors: Busse SC, Jue T
Traditionally, assigning the heme protein resonances has relied heavily on the comparison of spectra arising from protein reconstituted with specifically deuterated hemes and the native form. Such an approach can identify tentatively the broad, overlapping signals in the Fe(II) high-spin heme protein spectra. Although...
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[NMR paper] Proton NMR assignments of heme contacts and catalytically implicated amino acids in c
Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects.
Related Articles Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects.
Biochemistry. 1991 May 7;30(18):4398-405
Authors: Satterlee JD, Erman JE
Proton NMR assignments of the heme pocket and catalytically relevant...
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[NMR paper] The three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex by NMR spectr
The three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex by NMR spectroscopy.
J Mol Biol. 1999 Jun 11;289(3):529-45
Authors: Gruschus JM, Tsao DH, Wang LH, Nirenberg M, Ferretti JA
The three-dimensional solution structure obtained by NMR of the complex formed between the uniformly singly15N and doubly13C/15N-labeled...
1H NMR resonance assignments in a paramagnetic heme protein by two-dimensional spectr
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