Related ArticlesHigh resolution 2D-NMR studies indicating complete assignments and conformational characteristics of the NF-kappa B binding enhancer element of HIV-LTR.
J Biomol Struct Dyn. 1995 Oct;13(2):269-84
Authors: Singh MP, Fregeau NL, Pon RT, Lown JW
The asymmetrical DNA duplex [5'd(AAGGGACTTTCC)].[5'-d(GGAAAGTCCCTT)] has been studied by one- and two-dimensional NMR techniques. The sequence is comprised of the actual 10 base-pair long binding site for the transcription factor NF-kappa B in the enhancer sequence of the long term repeat (LTR) region of HIV and SIV types of retroviruses associated with the AIDS syndrome. Two additional A.T base-pairs are also included on one end for an added interest in the 12-bp duplex sequence with a pseudo dyad-symmetric disposition of the oligopurine and oligopyrimidine segments, as it appears in the HIV-1 genome. Phase-sensitive two-dimensional spectra (NOESY, ROESY, COSY and TOCSY) were obtained at three different temperatures (5, 15 and 25 degrees C) for a complete assignment of the non-exchangeable protons by tracing through sequence specific intra- and internucleotide connectivities. 2D-NOESY spectra were also acquired in aqueous (90% H2O-D2O) solutions, with two different methods of water signal suppression, to assign the exchangeable protons from specific NOE correlations. Adenine H2 protons were assigned by the use of NOE correlations and from T1 relaxation time measurements. The general spectral features and semi-quantitative interproton distance estimates indicate a B-DNA type conformation. However, some distinctly unusual features associated with the nucleotides at and immediately adjacent to both the 5'-and 3'-ends of AAA/TTT and GGG/CCC segments were noted. The complete assignments, and the observed characteristics, will be of significant value in studying the complexes of this transcriptionally active DNA domain with the protein and other rationally designed DNA binding agents.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
Bioorg Chem. 2011 Feb;39(1):59-66
Authors: Borioni A, Bastanzio G, Delfini M, Mustazza C, Sciubba F, Tatti M, Del Giudice MR
The interaction of new bivalent NOP receptor antagonists with dodecyl phosphatidylcholine micelles and DMPC/cholesterol liposomes was investigated in solution by high resolution NMR. The ligands are...
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[NMR paper] High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.
High-resolution solid-state NMR studies on uniformly -labeled ubiquitin.
Related Articles High-resolution solid-state NMR studies on uniformly -labeled ubiquitin.
Chembiochem. 2005 Sep;6(9):1638-47
Authors: Seidel K, Etzkorn M, Heise H, Becker S, Baldus M
Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly -labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the...
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[NMR paper] High-resolution NMR studies of encapsulated proteins in liquid ethane.
High-resolution NMR studies of encapsulated proteins in liquid ethane.
High-resolution NMR studies of encapsulated proteins in liquid ethane.
J Am Chem Soc. 2005 Jul 27;127(29):10176-7
Authors: Peterson RW, Lefebvre BG, Wand AJ
Many of the difficulties presented by large, aggregation-prone, and membrane proteins to modern solution NMR spectroscopy can be alleviated by actively seeking to increase the effective rate of molecular reorientation. An emerging approach involves encapsulating the protein of interest within the protective shell of a...
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[NMR paper] High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational vari
High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues.
Related Articles High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues.
J Mol Biol. 2003 Mar 21;327(2):507-20
Authors: Sprangers R, Groves MR, Sinning I, Sattler M
The SMN protein, which is linked to spinal muscular atrophy (SMA), plays an important role in the assembly of the...
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High-resolution methyl edited GFT NMR experiments for protein resonance assignments a
High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination
Abstract Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile, Leu, Met, Thr and Val) there is a significant overlap of 13C and 1H chemical shifts. Such overlap can be resolved using the recently proposed (3,2)D HCCH-COSY, a G-matrix Fourier transform (GFT) NMR based experiment, which facilitates editing...
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High-resolution methyl edited GFT NMR experiments for protein resonance assignments a
High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.
Related Articles High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.
J Biomol NMR. 2010 Sep 14;
Authors: Jaipuria G, Thakur A, D'Silva P, Atreya HS
Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile,...
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[NMR paper] High-resolution 1H- and 15N-NMR studies of Rhodospirillum rubrum cytochrome c2.
High-resolution 1H- and 15N-NMR studies of Rhodospirillum rubrum cytochrome c2.
Related Articles High-resolution 1H- and 15N-NMR studies of Rhodospirillum rubrum cytochrome c2.
Biochim Biophys Acta. 1991 May 23;1058(1):75-8
Authors: Smith GM, Yu LP
Rhodospirillum rubrum cytochrome c2 was uniformly enriched in 15N and studied by 1H- and 15N-NMR spectroscopy. Relaxation and NOE data allowed determination of the rotational correlation time and indicated more rapid side-chain motion in the native protein and increased segmental motion in the...
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Site-specific labeling of nucleotides for making RNA for high resolution NMR studies
Abstract Escherichia coli (E. coli) is a versatile organism for making nucleotides labeled with stable isotopes (13C, 15N, and/or 2H) for structural and molecular dynamics characterizations. Growth of a mutant E. coli strain deficient in the pentose phosphate pathway enzyme glucose-6-phosphate dehydrogenase (K10-1516) on 2-13C-glycerol and 15N-ammonium sulfate in Studier minimal medium enables labeling at sites useful for NMR spectroscopy. However, 13C-sodium formate combined with 13C-2-glycerol in the growth media adds labels to new positions. In the absence of labeled formate, both C5 and...
High resolution 2D-NMR studies indicating complete assignments and conformational cha
Linear Mode
