Related ArticlesAssignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronuclear NMR spectroscopy at natural abundance.
J Biomol NMR. 1994 Sep;4(5):689-702
Authors: Lefevre C, Adjadj E, Quiniou E, Mispelter J
Nearly complete assignment of the protonated carbon resonances of apo-neocarzinostatin, a 113-amino acid antitumor antibiotic carrier protein, has been achieved at natural 13C abundance using heteronuclear 2D experiments. Most of the cross peaks in the proton-carbon correlation map were identified by the combined use of HMQC, HMQC-RELAY and HMQC-NOESY spectra, using already published proton chemical shifts. However, double-DEPT and triple-quantum experiments had to be performed for the edition of CH and CH2 side-chain groups, respectively, which were hardly visible on HMQC-type maps. The triple-quantum pulse sequence was adapted from its original scheme to be applicable to a natural abundance sample. The correlation between carbon chemical shifts and the apo-neocarzinostatin structure is discussed. In particular, 13C alpha secondary shifts correlate well with the backbone conformation. These shifts also yield information about the main-chain flexibility of the protein. Assignments reported herein will be used further for interpretation of carbon relaxation times in a study of the internal dynamics of apo-neocarzinostatin.
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...
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NMR assignment of 1H, 13C, and 15N resonances of rat lipocalin-type prostaglandin D synthase.
NMR assignment of 1H, 13C, and 15N resonances of rat lipocalin-type prostaglandin D synthase.
NMR assignment of 1H, 13C, and 15N resonances of rat lipocalin-type prostaglandin D synthase.
Biomol NMR Assign. 2010 Oct;4(2):223-5
Authors: Liu J, Lv Y, Guo C, Lin D
Lipocalin-type prostaglandin D synthase (L-PGDS) acts as both a PGD(2)-synthesizing enzyme and an extracellular transporter for small lipophilic molecules. Here we report the backbone and side-chain resonance assignments of uniformly (15)N, (13)C labeled rat L-PGDS.
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[NMR paper] Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 d
Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy.
Related Articles Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy.
J Biomol NMR. 2000 Oct;18(2):173-6
Authors: Mulder FA, Ayed A, Yang D, Arrowsmith CH, Kay LE
The p53 tumor suppressor is a transcription factor that plays a crucial role in the activation of genes in response to DNA damage. As a first step towards detailed structural studies of the...
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[NMR paper] Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a dou
Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen.
FEBS Lett. 1995 Apr 10;362(3):333-6
Authors: Bycroft M, Proctor M, Freund SM, St Johnston D
NMR spectroscopy has been...
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[NMR paper] Assignment of the backbone 1H and 15N NMR resonances and secondary structure characte
Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar.
FEBS Lett. 1993 Oct 11;332(1-2):81-7
Authors: Lubienski MJ, Bycroft M, Jones DN, Fersht AR
Barstar, a polypeptide inhibitor of ribonucleases, has been studied by 2D and 3D NMR techniques using uniformly...
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[NMR paper] Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat
Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer.
Related Articles Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer.
Biochemistry. 1993 Aug 17;32(32):8322-8
Authors: van de Ven FJ, van Os JW, Aelen JM, Wymenga SS, Remerowski ML, Konings RN, Hilbers CW
The major coat protein (gVIIIp) of bacteriophage M13...
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[NMR paper] Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Related Articles Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Biochemistry. 1990 Jul 10;29(27):6341-62
Authors: McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW
The proton and nitrogen (15NH-H alpha-H beta) resonances of bacteriophage T4 lysozyme were assigned by 15N-aided 1H NMR. The assignments were directed from the backbone amide 1H-15N nuclei, with the heteronuclear single-multiple-quantum coherence (HSMQC)...
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Approaches to the assignment of 19F resonances from 3-fluorophenylalanine labeled cal
Abstract Traditional single site replacement mutations (in this case, phenylalanine to tyrosine) were compared with methods which exclusively employ 15N and 19F-edited two- and three-dimensional NMR experiments for purposes of assigning 19F NMR resonances from calmodulin (CaM), biosynthetically labeled with 3-fluorophenylalanine (3-FPhe). The global substitution of 3-FPhe for native phenylalanine was tolerated in CaM as evidenced by a comparison of 1H-15N HSQC spectra and calcium binding assays in the presence and absence of 3-FPhe. The 19F NMR spectrum reveals six resolved resonances, one...
Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronucle
Linear Mode
