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Kandala V. R. Chary - One of the best experts on this subject based on the ideXlab platform.
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Chemical shift based editing of CH_3 groups in fractionally ^13C-labelled proteins using GFT (3, 2)D CT-HCCH-COSY: stereospecific assignments of CH_3 groups of Val and Leu residues
Journal of Biomolecular NMR, 2008Co-Authors: Ravi Pratap Barnwal, Hanudatta S. Atreya, Kandala V. R. CharyAbstract:We propose a (3, 2)D CT-H CC H-COSY experiment to rapidly collect the data and provide significant dispersion in the spectral region containing ^13C–^1H cross peaks of CH_3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues. This enables one to carry out chemical shift based editing and grouping of all the ^13C–^1H cross peaks of CH_3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues in fractionally (10%) ^13C-labelled proteins, which in turn aids in the sequence-specific resonance assignments in general and side-chain resonance assignments in particular, in any given protein. Further, we demonstrate the utility of this experiment for stereospecific assignments of the pro -R and pro -S methyl groups belonging to the Leu and Val residues in fractionally (10%) ^13C-labelled proteins. The proposed experiment opens up a wide range of applications in resonance assignment strategies and structure determination of proteins.
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Chemical shift based editing of CH3 groups in fractionally 13C-labelled proteins using GFT (3, 2)D CT-HCCH-COSY: stereospecific assignments of CH3 groups of Val and Leu residues.
Journal of biomolecular NMR, 2008Co-Authors: Ravi Pratap Barnwal, Hanudatta S. Atreya, Kandala V. R. CharyAbstract:We propose a (3, 2)D CT-HCCH-COSY experiment to rapidly collect the data and provide significant dispersion in the spectral region containing 13C–1H cross peaks of CH3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues. This enables one to carry out chemical shift based editing and grouping of all the 13C–1H cross peaks of CH3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues in fractionally (10%) 13C-labelled proteins, which in turn aids in the sequence-specific resonance assignments in general and side-chain resonance assignments in particular, in any given protein. Further, we demonstrate the utility of this experiment for stereospecific assignments of the pro-R and pro-S methyl groups belonging to the Leu and Val residues in fractionally (10%) 13C-labelled proteins. The proposed experiment opens up a wide range of applications in resonance assignment strategies and structure determination of proteins.
Ravi Pratap Barnwal - One of the best experts on this subject based on the ideXlab platform.
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Chemical shift based editing of CH_3 groups in fractionally ^13C-labelled proteins using GFT (3, 2)D CT-HCCH-COSY: stereospecific assignments of CH_3 groups of Val and Leu residues
Journal of Biomolecular NMR, 2008Co-Authors: Ravi Pratap Barnwal, Hanudatta S. Atreya, Kandala V. R. CharyAbstract:We propose a (3, 2)D CT-H CC H-COSY experiment to rapidly collect the data and provide significant dispersion in the spectral region containing ^13C–^1H cross peaks of CH_3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues. This enables one to carry out chemical shift based editing and grouping of all the ^13C–^1H cross peaks of CH_3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues in fractionally (10%) ^13C-labelled proteins, which in turn aids in the sequence-specific resonance assignments in general and side-chain resonance assignments in particular, in any given protein. Further, we demonstrate the utility of this experiment for stereospecific assignments of the pro -R and pro -S methyl groups belonging to the Leu and Val residues in fractionally (10%) ^13C-labelled proteins. The proposed experiment opens up a wide range of applications in resonance assignment strategies and structure determination of proteins.
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Chemical shift based editing of CH3 groups in fractionally 13C-labelled proteins using GFT (3, 2)D CT-HCCH-COSY: stereospecific assignments of CH3 groups of Val and Leu residues.
Journal of biomolecular NMR, 2008Co-Authors: Ravi Pratap Barnwal, Hanudatta S. Atreya, Kandala V. R. CharyAbstract:We propose a (3, 2)D CT-HCCH-COSY experiment to rapidly collect the data and provide significant dispersion in the spectral region containing 13C–1H cross peaks of CH3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues. This enables one to carry out chemical shift based editing and grouping of all the 13C–1H cross peaks of CH3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues in fractionally (10%) 13C-labelled proteins, which in turn aids in the sequence-specific resonance assignments in general and side-chain resonance assignments in particular, in any given protein. Further, we demonstrate the utility of this experiment for stereospecific assignments of the pro-R and pro-S methyl groups belonging to the Leu and Val residues in fractionally (10%) 13C-labelled proteins. The proposed experiment opens up a wide range of applications in resonance assignment strategies and structure determination of proteins.
J. Michael Conlon - One of the best experts on this subject based on the ideXlab platform.
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Isolation of [Pro2,Met13]somatostatin-14 and somatostatin-14 from the frog brain reveals the existence of a somatostatin gene family in a tetrapod.
Biochemical and biophysical research communications, 1992Co-Authors: Hubert Vaudry, Nicolas Chartrel, J. Michael ConlonAbstract:Two somatostatin-related peptides were isolated in pure form from an extract of the brain of the European green frog, Rana ridibunda. The primary structure of the most abundant component was identical to that of mammalian somatostatin-14. The primary structure of the second component, present in approximately 5% of the abundance of somatostatin-14, was established as Ala-Pro-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Met-Cys. This sequence shows two substitutions (Pro for Gly2 and Met for Ser13) compared with mammalian somatostatin-14. The data provide evidence for a somatostatin gene family in tetrapods as well as in teleost fish.
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Primary structure of pancreatic polypeptide from four species of Perissodactyla (Przewalski's horse, zebra, rhino, tapir).
General and comparative endocrinology, 1991Co-Authors: J.steven Henry, Valentine A. Lance, J. Michael ConlonAbstract:Abstract Pancreatic polypeptide (PP) has been purified from extracts of the pancreas of four species of odd-toed ungulates (Perissodactyla): Przewalski's horse, mountain zebra, white rhinoceros, and mountain tapir. The amino acid sequence of Przewalski's horse pancreatic polypeptide was established as Ala-Pro-Met-Glu-Pro-Val-Tyr-Pro-Gly-Asp 10 -Asn-Ala-Thr- Pro-Glu-Gln-Met-Ala-Gln-Tyr 20 -Ala-Ala-Glu-Leu-Arg-Arg-Tyr-Ile-Asn-Met 30 -Leu-Thr-Arg-Pro-Arg-Tyr·NH 2 . Zebra PP was identical to Przewalski's horse PP, rhinoceros PP contained three substitutions relative to the horse (Ser for Ala 1 , Leu for Met 3 , and Glu for Gln 16 ), and tapir PP contained one substitution relative to the horse (Leu for Met 3 ). On the basis of morphological characteristics and the fossil record, the rhinocerotids are classified with the tapirids in the suborder Ceratomorpha, whereas the horse and zebra belong to a separate suborder, Hippomorpha. On the basis of structural similarity of the PP molecules, however, it would appear that the tapir is more closely related to the horse than to the rhinoceros. These observations provide a further example of the need for extreme caution when inferring taxonomic or phylogenetic relationships between species from the structures of homologous peptides.
Hanudatta S. Atreya - One of the best experts on this subject based on the ideXlab platform.
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Chemical shift based editing of CH_3 groups in fractionally ^13C-labelled proteins using GFT (3, 2)D CT-HCCH-COSY: stereospecific assignments of CH_3 groups of Val and Leu residues
Journal of Biomolecular NMR, 2008Co-Authors: Ravi Pratap Barnwal, Hanudatta S. Atreya, Kandala V. R. CharyAbstract:We propose a (3, 2)D CT-H CC H-COSY experiment to rapidly collect the data and provide significant dispersion in the spectral region containing ^13C–^1H cross peaks of CH_3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues. This enables one to carry out chemical shift based editing and grouping of all the ^13C–^1H cross peaks of CH_3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues in fractionally (10%) ^13C-labelled proteins, which in turn aids in the sequence-specific resonance assignments in general and side-chain resonance assignments in particular, in any given protein. Further, we demonstrate the utility of this experiment for stereospecific assignments of the pro -R and pro -S methyl groups belonging to the Leu and Val residues in fractionally (10%) ^13C-labelled proteins. The proposed experiment opens up a wide range of applications in resonance assignment strategies and structure determination of proteins.
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Chemical shift based editing of CH3 groups in fractionally 13C-labelled proteins using GFT (3, 2)D CT-HCCH-COSY: stereospecific assignments of CH3 groups of Val and Leu residues.
Journal of biomolecular NMR, 2008Co-Authors: Ravi Pratap Barnwal, Hanudatta S. Atreya, Kandala V. R. CharyAbstract:We propose a (3, 2)D CT-HCCH-COSY experiment to rapidly collect the data and provide significant dispersion in the spectral region containing 13C–1H cross peaks of CH3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues. This enables one to carry out chemical shift based editing and grouping of all the 13C–1H cross peaks of CH3 groups belonging to Ala, Ile, Leu, Met, Thr and Val residues in fractionally (10%) 13C-labelled proteins, which in turn aids in the sequence-specific resonance assignments in general and side-chain resonance assignments in particular, in any given protein. Further, we demonstrate the utility of this experiment for stereospecific assignments of the pro-R and pro-S methyl groups belonging to the Leu and Val residues in fractionally (10%) 13C-labelled proteins. The proposed experiment opens up a wide range of applications in resonance assignment strategies and structure determination of proteins.
Janusz Blasiak - One of the best experts on this subject based on the ideXlab platform.
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an association of polymorphism of dna repair genes xrcc1 and xrcc3 with colorectal cancer
Journal of Experimental & Clinical Cancer Research, 2004Co-Authors: Renata Krupa, Janusz BlasiakAbstract:: Variability in DNA repair genes may contribute to human cancer risk. We performed a case-control study (51 cases and 100 controls) to test the association between two polymorphisms: Arg399Gln in the XRCC1 gene and Thr241Met in the XRCC3 gene and colorectal cancer risk. Genotypes were determined in tumour tissue and distant mucosa samples by PCR RFLP with the NciI restriction enzyme for XRCC1 and NcoI for XRCC3. Cancer occurrence was strongly associated with the XRCC3 Met/Met polymorphic variant (OR = 9.45; (95% CI 8.77-11.65)), whereas Thr/Thr and Thr/Met variants were associated with significant reduction in colorectal cancer risk (OR = 0.16; 95% CI 0-0.26 and OR = 0.26; 95% CI 0.25-0.27, respectively). Weak association was found between the XRCC1 Arg/Arg and Gln/Gln variants and the risk of colorectal cancer (OR = 1.28; 95% CI 1.00-1.84 and OR = 1.13; 95% CI 0.85-2.34, respectively). Gene-gene interaction between the XRCC1 Arg/Arg and XRCC3 Met/Met homozygous variants slightly increased the risk (OR = 10.50; 95% CI 5.67-14.79). Both polymorphisms were not associated with colorectal cancer progression.