Related ArticlesAn NMR characterization of the regA protein-binding site of bacteriophage T4 gene 44 mRNA.
J Biol Chem. 1991 Sep 25;266(27):17832-7
Authors: Szewczak AA, Webster KR, Spicer EK, Moore PB
The conformations of two RNA dodecamers that differ markedly in affinity for the regA protein from bacteriophage T4 have been examined by NMR to see if the ability of that protein to discriminate between mRNAs is based on pre-existing differences in their three-dimensional structures. One of the RNAs examined has the same sequence as the site where regA protein binds when it inhibits the expression of gene 44's mRNA. The second RNA differs from the first in having a U instead of a G at position -9; it binds regA protein 100 times less tightly. The NMR data indicate that both RNAs have similar single-stranded conformations and that they each resemble an isolated strand of a double helix. They also show that most, if not all of the ribose rings in both molecules have appreciable 2'-endo puckering. It is unlikely that regA protein distinguishes between these two molecules on the basis of differences in their global conformations in solution.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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[NMR paper] Validation of the binding site structure of the cellular retinol-binding protein (CRB
Validation of the binding site structure of the cellular retinol-binding protein (CRBP) by ligand NMR chemical shift perturbations.
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J Am Chem Soc. 2005 Apr 20;127(15):5310-1
Authors: Wang B, Merz KM
We have calculated proton chemical shift perturbations (CSPs) of retinol in the cellular retinol-binding protein (CRBP) through the use of a recently developed computational approach (Wang et al. J....
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[NMR paper] Identification of the bile acid-binding site of the ileal lipid-binding protein by ph
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J Biol Chem. 2001 Mar 9;276(10):7291-301
Authors: Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C
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[NMR paper] An investigation of the ligand-binding site of the glutamine-binding protein of Esche
An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
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Biochemistry. 1994 Jul 26;33(29):8651-61
Authors: Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C
Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance...
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[NMR paper] Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with
Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with the aid of spin-labeled oligonucleotides in combination with 1H-NMR.
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Biochemistry. 1993 Sep 14;32(36):9407-16
Authors: Folkers PJ, van Duynhoven JP, van Lieshout HT, Harmsen BJ, van Boom JH, Tesser GI, Konings RN, Hilbers CW
The DNA binding domain of the single-stranded DNA binding protein...
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08-22-2010 03:01 AM
[NMR paper] An NMR characterization of the regA protein-binding site of bacteriophage T4 gene 44
An NMR characterization of the regA protein-binding site of bacteriophage T4 gene 44 mRNA.
Related Articles An NMR characterization of the regA protein-binding site of bacteriophage T4 gene 44 mRNA.
J Biol Chem. 1991 Sep 25;266(27):17832-7
Authors: Szewczak AA, Webster KR, Spicer EK, Moore PB
The conformations of two RNA dodecamers that differ markedly in affinity for the regA protein from bacteriophage T4 have been examined by NMR to see if the ability of that protein to discriminate between mRNAs is based on pre-existing differences in their...
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08-21-2010 11:12 PM
[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
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 Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Eur J Biochem. 1991 Aug 15;200(1):139-48
Authors: Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW
Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...
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[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
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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 Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Eur J Biochem. 1991 Aug 15;200(1):139-48
Authors: Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW
Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...
An NMR characterization of the regA protein-binding site of bacteriophage T4 gene 44
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