Related ArticlesInitiation sites of protein folding by NMR analysis.
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10600-3
Authors: Freund SM, Wong KB, Fersht AR
Detailed characterization of denatured states of proteins is necessary to understand the interactions that funnel the large number of possible conformations along fast routes for folding. Nuclear magnetic resonance experiments based on the nuclear Overhauser effect (NOE) detect hydrogen atoms close in space and provide information about local structure. Here we present an NMR procedure that detects almost all sequential NOEs between amide hydrogen atoms (HN-HN NOE), including those in random coil regions in a protein, barnase, in urea solutions. A semi-quantitative analysis of these HN-HN NOEs identified partly structured regions that are in remarkable agreement with those found to form early on the reaction pathway. Our results strongly suggest that the folding of barnase initiates at the first helix and the beta-turn between the third and the fourth strands. This strategy of defining residual structure has also worked for cold-denatured barstar and guanidinium hydrochloride-denatured chymotrypsin inhibitor 2 and so should be generally applicable.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Bioorg Med Chem. 2011 Aug 27;
Authors: Masuda Y, Fukuchi M, Yatagawa T, Tada M, Takeda K, Irie K, Akagi KI, Monobe Y, Imazawa T, Takegoshi K
Abstract
Aggregation of 42-residue amyloid ?-protein (A?42) plays a pivotal role in the etiology of Alzheimer's disease (AD). Curcumin, the yellow pigment in the rhizome of turmeric, attracts...
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[NMR paper] NMR analysis of intra- and inter-molecular stems in the dimerization initiation site
NMR analysis of intra- and inter-molecular stems in the dimerization initiation site of the HIV-1 genome.
Related Articles NMR analysis of intra- and inter-molecular stems in the dimerization initiation site of the HIV-1 genome.
J Biochem. 2000 Apr;127(4):681-6
Authors: Takahashi K, Baba S, Hayashi Y, Koyanagi Y, Yamamoto N, Takaku H, Kawai G
Two positive-strand HIV-1 genomic RNAs form a dimer in virion particles through interaction of the dimerization initiation sites (DIS). The DIS RNA fragment spontaneously formed a "loose-dimer" and was...
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NMR Studies of Translocation of the Zif268 Protein between Its Target DNA Sites
NMR Studies of Translocation of the Zif268 Protein between Its Target DNA Sites
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100962h/aop/images/medium/bi-2010-00962h_0005.gifBiochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
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[NMR paper] Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spec
Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Related Articles Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Int J Pept Protein Res. 1996 Apr;47(4):282-8
Authors: Katahira R, Flotow H, Thomas G, Nosaka AY
An increase in the rate of protein synthesis is found to be accompanied by phosphorylation of the 40S ribosomal protein S6. Treatment of S6 by cyanogen bromide produced three fragments, and one of the fragments of S6, which is a C-terminal...
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[NMR paper] Dynamic NMR spectral analysis and protein folding: identification of a highly populat
Dynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Dynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR.
Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7222-6
Authors: Ropson IJ, Frieden C
...
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[NMR paper] Identification of the ribosome binding sites of translation initiation factor IF3 by
Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy.
RNA. 1999 Jan;5(1):82-92
Authors: Sette M, Spurio R, van Tilborg P, Gualerzi CO, Boelens R
Titrations of Escherichia coli translation initiation...
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NMR studies of translocation of the Zif268 protein between its target DNA sites.
NMR studies of translocation of the Zif268 protein between its target DNA sites.
Related Articles NMR studies of translocation of the Zif268 protein between its target DNA sites.
Biochemistry. 2010 Aug 19;
Authors: Takayama Y, Sahu D, Iwahara J
Zif268 is a zinc-finger protein containing three Cys2-His2-type zinc-finger domains that bind the target DNA sequence GCGTGGGCG in a cooperative manner. In this work, we characterized translocation of the Zif268 protein between its target DNA sites using NMR spectroscopy. The residual dipolar coupling...
Initiation sites of protein folding by NMR analysis.
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