[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 of hydrogen bonding in cold-shock protein A and an analysis of the influence of c
NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths.
Related Articles NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths.
Protein Sci. 2001 Sep;10(9):1856-68
Authors: Alexandrescu AT, Snyder DR, Abildgaard F
Hydrogen bonding in cold-shock protein A of Escherichia coli has been investigated using long-range HNCO spectroscopy. Nearly half of the...
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11-19-2010 08:44 PM
[NMR paper] Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium
Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Related Articles Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Eur J Biochem. 2001 May;268(9):2527-39
Authors: Kremer W, Schuler B, Harrieder S, Geyer M, Gronwald W, Welker C, Jaenicke R, Kalbitzer HR
Cold-shock proteins (Csps) are a subgroup of the cold-induced proteins preferentially expressed in bacteria and other organisms on reduction of the growth temperature below the...
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[NMR paper] NMR backbone assignments of the cold-regulated RNA-binding protein, rbpA1, in the cya
NMR backbone assignments of the cold-regulated RNA-binding protein, rbpA1, in the cyanobacterium, anabaena variabilis M3.
Related Articles NMR backbone assignments of the cold-regulated RNA-binding protein, rbpA1, in the cyanobacterium, anabaena variabilis M3.
J Biomol NMR. 2000 Aug;17(4):351-2
Authors: Morita EH, Murakami T, Uegaki K, Yamazaki T, Sato N, Kyogoku Y, Hayashi H
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[NMR paper] Microscopic stability of cold shock protein A examined by NMR native state hydrogen e
Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Related Articles Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Protein Sci. 2000 Feb;9(2):290-301
Authors: Jaravine VA, Rathgeb-Szabo K, Alexandrescu AT
Native state hydrogen exchange of cold shock protein A (CspA) has been characterized as a function of the denaturant urea and of the stabilizing agent...
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11-18-2010 09:15 PM
[NMR paper] NMR assignments for acid-denatured cold shock protein A.
NMR assignments for acid-denatured cold shock protein A.
Related Articles NMR assignments for acid-denatured cold shock protein A.
J Biomol NMR. 1998 May;11(4):461-2
Authors: Alexandrescu AT, Rathgeb-Szabo K
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[NMR paper] Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli:
Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
Proc Natl Acad Sci U S A. 1994 May 24;91(11):5114-8
Authors: Newkirk K, Feng W, Jiang W, Tejero R, Emerson SD, Inouye M, Montelione GT
Sequence-specific...
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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...