Cell signaling, post-translational protein modifications and NMR spectroscopy
Cell signaling, post-translational protein modifications and NMR spectroscopy
Abstract Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities such as phosphate-, acyl-, alkyl- and glycosyl-groups onto selected subsets of modifiable amino acids. In turn, these modifications induce highly specific changes in the chemical ...
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09-29-2012 11:56 AM
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Biomol NMR Assign. 2011 Jul 6;
Authors: Veith T, Wurm JP, Duchardt-Ferner E, Weis B, Martin R, Safferthal C, Bohnsack MT, Schleiff E, Wöhnert J
Eukaryotic ribosome biogenesis requires the concerted action of ~200 auxiliary protein factors on the nascent ribosome. For many of these...
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07-07-2011 05:12 PM
[NMR paper] NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Therm
NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
Related Articles NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
J Biomol NMR. 2005 Jan;31(1):73-4
Authors: Grimm SK, Wöhnert J
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[NMR paper] Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation p
Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
Related Articles Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
J Mol Biol. 2003 Mar 21;327(2):521-36
Authors: Huang YJ, Swapna GV, Rajan PK, Ke H, Xia B, Shukla K, Inouye M, Montelione GT
Ribosome-binding factor A (RbfA) from Escherichia coli is a cold-shock adaptation protein. It is essential for efficient processing of 16S rRNA and is suspected to interact with...
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11-24-2010 09:01 PM
[NMR paper] NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly
NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
Related Articles NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
J Mol Biol. 2002 Oct 11;323(1):143-51
Authors: Raibaud S, Lebars I, Guillier M, Chiaruttini C, Bontems F, Rak A, Garber M, Allemand F, Springer M, Dardel F
L20 is a specific protein of the bacterial ribosome, which is involved in the early assembly steps of the 50S subunit and in the feedback control of the...
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11-24-2010 08:58 PM
[NMR paper] Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N r
Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
Related Articles Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
J Am Chem Soc. 2001 Feb 7;123(5):967-75
Authors: Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE
A new NMR experiment is presented for...
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11-19-2010 08:32 PM
[NMR paper] K(+)-ribosome interactions determine the large enhancements of 39K NMR transverse rel
K(+)-ribosome interactions determine the large enhancements of 39K NMR transverse relaxation rates in the cytoplasm of Escherichia coli K-12.
Related Articles K(+)-ribosome interactions determine the large enhancements of 39K NMR transverse relaxation rates in the cytoplasm of Escherichia coli K-12.
Biochemistry. 1995 Jan 31;34(4):1393-404
Authors: Guttman HJ, Cayley S, Li M, Anderson CF, Record MT
As a probe of physical chemical properties of the intracellular environment, we measured 39K NMR transverse relaxation rates in concentrated cell...
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08-22-2010 03:41 AM
[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...
Co-Translational Protein Folding on the Ribosome: using NMR Spectroscopy to Provide Structure and Dynamics of Ribosome-Nascent Chains
Linear Mode
