Related ArticlesNMR study into the mechanism of recognition of the degree of polymerization by oligo/polysialic acid antibodies.
Bioorg Med Chem. 2013 Oct 1;21(19):6069-76
Authors: Hanashima S, Sato C, Tanaka H, Takahashi T, Kitajima K, Yamaguchi Y
Abstract
Oligo/polysialic acids consisting of consecutive ?(2,8)-linkages on gangliosides and glycoproteins play a role in cell adhesion and differentiation events in a manner that is dependent on the degree of polymerization (DP). Anti-oligo/polysialic acid antibodies often have DP-dependent antigenic specificity, and such unique antibodies are often used in biological studies for the detection and differentiation of oligo/polysialic acids. However, molecular mechanisms remain unclear. We here use NMR techniques to analyze the binding epitopes of the anti-oligo/polysialic acid monoclonal antibodies (mAb) A2B5 and 12E3. The mAb A2B5, which has a preference for trisialic acid, recognizes sialic acid residues at the non-reducing terminus and those in nascent units. On the other hand, mAb 12E3, which prefers oligo/polysialic acids of more than six sugar units, recognizes inner sialic acid residues. In both structural complexes, the interresidue transferred NOE correlations are significantly different from those arising from analogs of the free states, indicating that the bound and free sugar conformations are distinct. The ability of the two mAbs to distinguish the chain lengths comes from different binding epitopes and possibly from the conformational differences in the oligo/polysialic acids. Information on the recognition modes is needed for the structural design of immunoreactive antigens for the development of high-affinity anti-polysialic acid antibodies and of related vaccines against pathogenic, polysialic acid-coated bacteria.
[NMR paper] Natural compounds against Alzheimer's disease: molecular recognition of A?1-42 peptide by Salvia sclareoides extract and its major component, rosmarinic acid, as investigated by NMR.
Natural compounds against Alzheimer's disease: molecular recognition of A?1-42 peptide by Salvia sclareoides extract and its major component, rosmarinic acid, as investigated by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Natural compounds against Alzheimer's disease: molecular recognition of A?1-42 peptide by Salvia sclareoides extract and its major component, rosmarinic acid, as investigated by NMR.
Chem Asian J. 2013 Mar;8(3):596-602
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Formation of Trivalent Zirconocene Complexes from ansa-Zirconocene-Based Olefin-Polymerization Precatalysts: An EPR- and NMR-Spectroscopic Study
Formation of Trivalent Zirconocene Complexes from ansa-Zirconocene-Based Olefin-Polymerization Precatalysts: An EPR- and NMR-Spectroscopic Study
Taylor N. Lenton, John E. Bercaw, Valentina N. Panchenko, Vladimir A. Zakharov, Dmitrii E. Babushkin, Igor E. Soshnikov, Evgenii P. Talsi and Hans H. Brintzinger
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja403170u/aop/images/medium/ja-2013-03170u_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja403170u
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
[NMR paper] Solution NMR study of DNA recognition mechanism of IRF4 protein.
Solution NMR study of DNA recognition mechanism of IRF4 protein.
Related Articles Solution NMR study of DNA recognition mechanism of IRF4 protein.
Nucleic Acids Symp Ser (Oxf). 2004;(48):105-6
Authors: Ishizaki I, Nomura M, Yamamoto K, Matsuyama T, Mishima M, Kojima C
Transcription factor IRF-4 prefers the DNA sequence including CCGAAA. The consensus sequence of the IRF family proteins is NNGAAA, and all crystal structures indicate the NN region does not interact with IRF proteins directly. Here the sequence preference of IRF-4 was...
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[NMR paper] Intestinal fatty acid binding protein: the folding mechanism as determined by NMR stu
Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Related Articles Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Biochemistry. 2001 Jan 23;40(3):732-42
Authors: Hodsdon ME, Frieden C
The intestinal fatty acid binding protein is composed of two beta-sheets surrounding a large interior cavity. There is a small helical domain associated with the portal for entry of the ligand into the cavity. Denaturation of the protein has been monitored in a residue-specific...
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[NMR paper] Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation
Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
Arch Biochem Biophys. 1993 Mar;301(2):244-50
Authors: Desideri A, Polticelli F, Falconi M, Sette M, Ciriolo MR, Paci M,...
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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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NMR post-doc position: NMR-based dynamics study of enzyme mechanism
The following post-doc position in NMR is available in University of Missouri:
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We have an opening for a postdoctoral fellow to use NMR to study dynamics of an enzyme while it is carrying on reversible catalysis. The prospects are promising and can be compared with thorough enzymology and crystallography of its ligand-dependent conformational changes (done in our dept.). The enzyme is sizeable enough to be challenging, but we have a battery of excellent 800 MHz spectra of deuterated samples for launching the project. The postdoctoral fellow will be housed in a new...