INTERTEK GROUP PLC : Intertek Expands cGMP Protein Structure Characterization ... - 4-traders
INTERTEK GROUP PLC : Intertek Expands cGMP Protein Structure Characterization ... - 4-traders
INTERTEK GROUP PLC : Intertek Expands cGMP Protein Structure Characterization ... 4-traders ... biosimilars to explore the secondary and tertiary structure of proteins. In line with ICH Q6B guidelines, Intertek now offer a comprehensive set of higher order structure techniques, including CD, such as FTIR, NMR and Fluorescence spectroscopy.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Tomasz L. Religa, Amy M. Ruschak, Rina Rosenzweig and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202259a/aop/images/medium/ja-2011-02259a_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202259a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/rQfCMlQFoW8
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05-20-2011 09:17 PM
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
J Am Chem Soc. 2011 May 11;
Authors: Religa TL, Ruschak AM, Rosenzweig R, Kay LE
Methyl groups are powerful reporters of structure, motion and function in NMR studies of supra-molecular protein assemblies. Their...
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05-12-2011 03:40 PM
[NMR paper] Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Related Articles Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Protein Sci. 2005 Sep;14(9):2421-8
Authors: Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ
Coiled-coil motifs play essential roles in protein assembly and molecular recognition, and are therefore the targets of many ongoing...
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12-01-2010 06:56 PM
[NMR paper] Structural difference between group I and group II cobra cardiotoxins: X-ray, NMR, an
Structural difference between group I and group II cobra cardiotoxins: X-ray, NMR, and CD analysis of the effect of cis-proline conformation on three-fingered toxins.
Related Articles Structural difference between group I and group II cobra cardiotoxins: X-ray, NMR, and CD analysis of the effect of cis-proline conformation on three-fingered toxins.
Biochemistry. 2005 May 24;44(20):7414-26
Authors: Chen TS, Chung FY, Tjong SC, Goh KS, Huang WN, Chien KY, Wu PL, Lin HC, Chen CJ, Wu WG
Natural homologues of cobra cardiotoxins (CTXs) were...
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11-25-2010 08:21 PM
[NMR paper] NMR characterization of residual structure in the denatured state of protein L.
NMR characterization of residual structure in the denatured state of protein L.
Related Articles NMR characterization of residual structure in the denatured state of protein L.
J Mol Biol. 2000 Jun 23;299(5):1341-51
Authors: Yi Q, Scalley-Kim ML, Alm EJ, Baker D
Triple-resonance NMR experiments were used to assign the (13)C(alpha), (13)C(beta), (15)N and NH resonances for all the residues in the denatured state of a destabilized protein L variant in 2 M guanidine. The chemical shifts of most resonances were very close to their random coil...
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11-18-2010 09:15 PM
[NMR paper] Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequen
Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide.
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 Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and...
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08-22-2010 03:33 AM
[NMR paper] Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequen
Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide.
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 Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and...
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08-22-2010 03:33 AM
[NMR paper] Ribosomal protein S17: characterization of the three-dimensional structure by 1H and
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Related Articles Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Biochemistry. 1993 Nov 30;32(47):12812-20
Authors: Golden BL, Hoffman DW, Ramakrishnan V, White SW
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a...