Related ArticlesOrientation and mobility of the heme vinyl groups in myoglobins with the aid of NOE and MATDUHM NMR.
Biochim Biophys Acta. 1992 Apr 8;1120(2):173-82
Authors: Yamamoto Y, Iwafune K, Nanai N, Chûjô R, Inoue Y, Suzuki T
The heme vinyl substituents in a shark (Galeorhinus japonicus) myoglobin in its met-cyano form (MbCN) have been characterized by NMR and the results were compared with those of the well-studied sperm whale (Physter catodon) myoglobin. Their orientation has been inferred from NOE connectivities and the analysis of the hyperfine shifts based on the principal magnetic tensor determined by MATDUHM (Magnetic Anisotropy Tensor Orientation Determination Utilizing the Heme Methyls) [Yamamoto, Y., Nanai, N. and Chujo, R.(1990) J. Chem. Soc., Chem. Commun. 1556-1557]. It has been shown that the C3-vinyl group is oriented roughly orthogonal to the heme plane in both G. japonicus and P. catodon MbCNs at 35 degrees C and their C8-vinyl groups, on the other hand, are close to in-plane orientation. Although CO form of myoglobin (MbCO) and MbCN have been thought to be isostructural to each other, the C8-vinyl orientation for P. catodon MbCN is found to be different from the orthogonal orientation indicated in the crystal structure analysis of MbCO [Hanson, J.C. and Schoenborn, B.P. (1981) J. Mol. Biol. 153, 117-146]. Their mobility has been characterized quantitatively from the study of time-dependent NOE build-up between the selected pair of the vinyl proton resonances. It has been revealed that the heme C3- and C8-vinyl groups of approximately 1 mM G. japonicus MbCN at 45 degrees C undergo internal motion with the correlation time of 1.9 and 2.4 ns, respectively. Therefore, their oscillatory motion is faster by a factor of 4-5 compared with the protein overall tumbling. Difference in the internal mobility between the two vinyl groups in the active site of this Mb is attributed to their differential contact with the apo-protein.
[NMR paper] Direct determination of changes of interdomain orientation on ligation: use of the or
Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32).
Related Articles Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32).
Biochemistry. 1999 Aug 10;38(32):10225-30
Authors: Fushman D, Xu R, Cowburn D
The relative orientation and motions of domains within many proteins are key to the control of multivalent recognition, or the assembly of protein-based cellular...
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11-18-2010 08:31 PM
[Question from NMRWiki Q&A forum] How to determine physical orientation of X and Y shims?
How to determine physical orientation of X and Y shims?
Hello, I need to help solids lab at our UCI site - they have a custom probe and need to orient it properly in order to ease the shimming procedure.
My question is - how to determine orientation of X and Y shims?
We have 800 MHz 63 mm Oxford magnet (+ Varian UnityInova console)
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09-14-2010 03:44 AM
[NMR paper] H NMR probes for inter-segmental hydrogen bonds in myoglobins.
H NMR probes for inter-segmental hydrogen bonds in myoglobins.
Related Articles H NMR probes for inter-segmental hydrogen bonds in myoglobins.
J Biochem. 1996 Jul;120(1):126-32
Authors: Yamamoto Y
NMR signals arising from the HisB5 N delta H and HisEF5 N epsilon H protons in sperm whale skeletal and horse heart myoglobins have been located for the first time in the downfield shifted portion of the spectra. The shifts and hydrogen exchange rates indicate that these His imidazole ring NH protons are involved in the inter-segmental hydrogen bonds...
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08-22-2010 02:27 PM
[NMR paper] Effect of bacteriorhodopsin on the orientation of the headgroup of 1,2-dimyristoyl-sn
Effect of bacteriorhodopsin on the orientation of the headgroup of 1,2-dimyristoyl-sn-glycero-3-phosphocholine in bilayers: a 31P- and 2H-NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Effect of bacteriorhodopsin on the orientation of the headgroup of 1,2-dimyristoyl-sn-glycero-3-phosphocholine in bilayers: a 31P- and 2H-NMR study.
Biochim Biophys Acta. 1992 May 21;1106(2):317-24
Authors: Gale P, Watts A
Bacteriorhodopsin (BR), purified from the halophilic...
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08-21-2010 11:41 PM
[NMR paper] 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket st
1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Related Articles 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Biochemistry. 1991 Feb 19;30(7):1878-87
Authors: Lee KB, La Mar GN, Pandey RK, Rezzano IN, Mansfield KE, Smith KM
1H nuclear magnetic resonance spectroscopy was used to assign the hyperfine-shifted resonances and determine the position of...
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[NMR paper] 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm w
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
Biochim Biophys Acta. 1990 Nov 15;1041(2):186-94
Authors: Hauksson JB, La Mar GN, Pande U, Pandey RK, Parish DW, Singh JP, Smith KM
The...
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08-21-2010 11:04 PM
[NMR paper] 1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorh
1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorhinus japonicus.
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 1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorhinus japonicus.
Eur J Biochem. 1990 May 20;189(3):567-73
Authors: Yamamoto Y, Inoue Y, Chûjô R, Suzuki T
Time-dependent NOE studies of the C13(1) and C17(1) methylene proton resonances of the heme...
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Module 1.0 - domain orientation with RDC data
Module 1.0 - interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings.
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