Related ArticlesNMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Biochemistry. 1990 Apr 10;29(14):3509-14
Authors: Redfield AG, Papastavros MZ
The structure of the phosphoryl binding region of human N-ras p21 was probed by using heteronuclear proton-observed NMR methods. Normal protein and a Gly-12----Asp-12 mutant protein were prepared with two amino acids labeled with 15N at their amide positions: valine and glycine, aspartic acid and glycine, and lysine and glycine. We completed the identification of amide 15NH resonances from Gly-12 and Asp-12 to the end of the phosphoryl binding domain consensus sequence (Lys-16) in protein complexed with GDP and have made tentative amide identifications from Val-9 to Ser-17. The methods used, together with initial identifications of the Gly-12 and -13 amide resonances, were described previously [Campbell-Burk, S. (1989) Biochemistry 28, 9478-9484]. The amide resonances of both Gly-13 and Lys-16 are shifted downfield below 10.4 ppm in both the normal and mutant proteins. These downfield shifts are presumed to be due to strong hydrogen bonds with the beta-phosphate oxygens of GDP.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Biochem Biophys Res Commun. 2010 Dec 24;
Authors: Myint W, Gong Q, Ahn J, Ishima R
Sarcoplasmic reticulum Ca(2+) ATPase (SERCA) is essential for muscle function by transporting Ca(2+) from the cytosol into the sarcoplasmic reticulum through ATP hydrolysis. In this report, the effects of substitution mutations on the...
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[NMR paper] NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus t
NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.
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J Biol Chem. 2004 Aug 6;279(32):33958-67
Authors: Revington M, Holder TM, Zuiderweg ER
We present an NMR investigation of the nucleotide-dependent conformational properties of a 44-kDa nucleotide binding...
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[NMR paper] Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of mu
Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.
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Biochem J. 2003 Dec 15;376(Pt 3):749-56
Authors: Ramaen O, Masscheleyn S, Duffieux F, Pamlard O, Oberkampf M, Lallemand JY, Stoven V, Jacquet E
Multidrug-resistance-associated...
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[NMR paper] Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubu
Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods.
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Physiol Chem Phys Med NMR. 2001;33(2):139-51
Authors: Kuchroo K, Maity H, Kasturi SR
Tubulin, the major protein of microtubules, has been shown to be an example of protein undergoing multistep unfolding. Local unfolding and stepwise loss of a...
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[NMR paper] Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP inte
Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae.
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Biochem J. 1998 Sep 15;334 ( Pt 3):601-7
Authors: Miller RW, Eady RR, Gormal C, Fairhurst SA, Smith BE
Investigation of the interaction of MgADP- and MgATP2- with the Fe protein of Klebsiella pneumoniae nitrogenase by 31P NMR showed that the adenine...
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[NMR paper] Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as mo
Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
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Eur J Biochem. 1993 Apr 15;213(2):781-8
Authors: Löw A, Sprinzl M, Limmer S
Proton-NMR signals in the downfield region (below approximately 10...
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[NMR paper] Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophil
Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
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Biochemistry. 1992 Mar 24;31(11):2970-7
Authors: Limmer S, Reiser CO, Schirmer NK, Grillenbeck NW, Sprinzl M
Proton NMR experiments of the GTP/GDP-binding protein EF-Tu from the extremely thermophilic bacterium Thermus thermophilus HB8 in H2O have been performed paying special attention to the...
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[NMR paper] Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV
Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nsb.gif Related Articles Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
Nat Struct Biol. 1999 Feb;6(2):141-5
Authors: Weliky DP, Bennett AE, Zvi A, Anglister J, Steinbach PJ, Tycko R
Solid-state NMR measurements have been carried out on frozen solutions of the complex of a 24-residue peptide derived from the third variable...
NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for
Linear Mode
