Relevant bibliographies by topics / Terminal and internal amino and amidoalkynes

Academic literature on the topic 'Terminal and internal amino and amidoalkynes'

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Published: 4 June 2021
Last updated: 21 February 2023

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Journal articles on the topic "Terminal and internal amino and amidoalkynes"

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Sjöquist, J., and C. B. Laurell. "N-Terminal Amino Acids of Isolated M-components." Acta Medica Scandinavica 170, S367 (April 24, 2009): 65–68. http://dx.doi.org/10.1111/j.0954-6820.1961.tb12424.x.

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Nethery, Kimberly A., C. Kuyler Doyle, Xiaofeng Zhang, and Jere W. McBride. "Ehrlichia canis gp200 Contains Dominant Species-Specific Antibody Epitopes in Terminal Acidic Domains." Infection and Immunity 75, no. 10 (August 6, 2007): 4900–4908. http://dx.doi.org/10.1128/iai.00041-07.

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ABSTRACT Species-specific antibody epitopes within several major immunoreactive protein orthologs of Ehrlichia species have recently been identified and molecularly characterized. In this study, dominant B-cell epitopes within the acidic (pI 5.35) ankyrin repeat-containing 200-kDa major immunoreactive protein (gp200) of Ehrlichia canis were defined. The E. canis gp200 gene (4,263 bp; 1,421 amino acids) was cloned and expressed as four (N-terminal, 1,107 bp; N-internal, 910 bp; C-internal, 1,000 bp; and C-terminal, 1,280 bp) overlapping recombinant proteins. The N-terminal, C-internal, and C-terminal polypeptides (369, 332, and 426 amino acids, respectively) were strongly recognized by antibody, and the major epitope(s) in these polypeptides was mapped to four polypeptide regions (40 to 70 amino acids). Smaller overlapping recombinant polypeptides (14 to 15 amino acids) spanning these regions identified five strongly immunoreactive species-specific epitopes that exhibited conformational dependence. The majority of the epitopes (four) were located in two strongly acidic (pI 4 to 4.9) domains in the distal N- and C-terminal regions of the protein flanking the centralized ankyrin domain-containing region. The amino acid content of the epitope-containing domains included a high proportion of strongly acidic amino acids (glutamate and aspartate), and these domains appear to have important biophysical properties that influence the antibody response to gp200.
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Wright, Sue P., Tim C. R. Prickett, Robert N. Doughty, Chris Frampton, Greg D. Gamble, Tim G. Yandle, Norman Sharpe, and Mark Richards. "Amino-Terminal Pro–C-Type Natriuretic Peptide in Heart Failure." Hypertension 43, no. 1 (January 2004): 94–100. http://dx.doi.org/10.1161/01.hyp.0000105623.04382.c0.

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Hamilton, VaNae, Ujjal K. Singha, Joseph T. Smith, Ebony Weems, and Minu Chaudhuri. "Trypanosome Alternative Oxidase Possesses both an N-Terminal and Internal Mitochondrial Targeting Signal." Eukaryotic Cell 13, no. 4 (February 21, 2014): 539–47. http://dx.doi.org/10.1128/ec.00312-13.

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ABSTRACTRecognition of mitochondrial targeting signals (MTS) by receptor translocases of outer and inner membranes of mitochondria is one of the prerequisites for import of nucleus-encoded proteins into this organelle. The MTS for a majority of trypanosomatid mitochondrial proteins have not been well defined. Here we analyzed the targeting signal for trypanosome alternative oxidase (TAO), which functions as the sole terminal oxidase in the infective form ofTrypanosoma brucei. Deleting the first 10 of 24 amino acids predicted to be the classical N-terminal MTS of TAO did not affect its import into mitochondriain vitro. Furthermore, ectopically expressed TAO was targeted to mitochondria in both forms of the parasite even after deletion of first 40 amino acid residues. However, deletion of more than 20 amino acid residues from the N terminus reduced the efficiency of import. These data suggest that besides an N-terminal MTS, TAO possesses an internal mitochondrial targeting signal. In addition, both the N-terminal MTS and the mature TAO protein were able to target a cytosolic protein, dihydrofolate reductase (DHFR), to aT. bruceimitochondrion. Further analysis identified a cryptic internal MTS of TAO, located within amino acid residues 115 to 146, which was fully capable of targeting DHFR to mitochondria. The internal signal was more efficient than the N-terminal MTS for import of this heterologous protein. Together, these results show that TAO possesses a cleavable N-terminal MTS as well as an internal MTS and that these signals act together for efficient import of TAO into mitochondria.
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Campbell, Duncan J., Anthony J. Valentijn, and Rosemary Condron. "Purification and amino-terminal sequence of rat kidney renin." Journal of Hypertension 9, no. 1 (January 1991): 29–34. http://dx.doi.org/10.1097/00004872-199101000-00005.

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Campbell, Duncan J., Anthony J. Valentijn, and Rosemary Condron. "Purification and amino-terminal sequence of rat kidney renin." Journal of Hypertension 9, no. 1 (1991): 29???34. http://dx.doi.org/10.1097/00004872-199109010-00005.

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Buhi, W. C., I. M. Alvarez, V. M. Shille, M. J. Thatcher, J. P. Harney, and M. Cotton. "Purification and characterization of a uterine retinol-binding protein in the bitch." Biochemical Journal 311, no. 2 (October 15, 1995): 407–15. http://dx.doi.org/10.1042/bj3110407.

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A major canine endometrial secreted protein (cP6, 23,000-M(r)) was purified by ion-exchange and gel-filtration chromatography and characterized by two-dimensional gel electrophoresis. Anti-[human retinol-binding protein (hRBP)] serum identified cP6 on immunoblot analysis and immunoprecipitated cP6 from culture medium. This major protein was also shown to bind [3H]retinol. N-terminal and internal amino acid sequences were determined and compared with previously identified protein, RNA, or DNA sequences. N-terminal analysis revealed that cP6 had high identity and similarity to serum retinol-binding proteins (RBPs), while internal sequence analysis showed a strong similarity to rat androgen-dependent epididymal protein and beta-lactoglobulins. Amino acid analysis, however, showed significant differences between these proteins and cP6 in both total amino acid content and certain selected amino acids. Immunohistochemical analysis showed staining for RBP only in the uterine luminal epithelium. These studies suggest that bitch endometrium secretes a family of proteins (cP6), some of which bind [3H]retinol, are immunologically related to the RBP family, and have N-terminal and internal sequences with a high similarity to RBP, beta-lactoglobulins and other members of the lipocalin family. This family of proteins may be important in early development for supplying retinol or derivatives to the developing embryo.
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Sanchez, Aniel, Yassel Ramos, Yanni Solano, Luis Javier González, Lazaro Betancourt, Jeovanis Gil, Gabriel Padron, and Vladimir Besada. "Letter: Specific Isotope Labeling for the Identification of Free N-Terminal Peptides of Proteins Separated by Polyacrylamide Gel Electrophoresis." European Journal of Mass Spectrometry 13, no. 4 (August 2007): 307–9. http://dx.doi.org/10.1255/ejms.880.

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We report here a method for the identification of free N-terminal peptides of in gel digested isolated proteins. It is based on the difference between the isotopic ion distribution of the N-terminal peptide and internal peptides. After guanidination of lysine residues, the primary amino groups of the gel-entrapped protein are blocked with an equimolar mixture of normal and deuterated acetic anhydride. Upon MS analysis, internal peptides display a normal isotopic ion distribution while the N-terminal peptide shows a complex isotopic ion distribution.
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Li, Wen-Yi, Fu-Chun Chiu, Yu-Fen Chien, Jou-Wei Lin, and Juey-Jen Hwang. "Association of Amino-terminal Pro-brain Natriuretic Peptide with Metabolic Syndrome." Internal Medicine 50, no. 11 (2011): 1143–47. http://dx.doi.org/10.2169/internalmedicine.50.4765.

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MOREIRA, C., F. SEREJO, P. ALCANTARA, M. GATOVARELA, C. SALDANHA, and J. BRAZNOGUEIRA. "Ambulatory blood pressure, procolagen amino-terminal polypeptide (P-III-P) and hemorreologyc parameters." American Journal of Hypertension 18, no. 5 (May 2005): A154—A155. http://dx.doi.org/10.1016/j.amjhyper.2005.03.429.

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Dissertations / Theses on the topic "Terminal and internal amino and amidoalkynes"

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Shasha, Adelle. "Metal-Catalysed Hydroamination." Science. School of Chemistry, 2007. http://hdl.handle.net/2123/1710.

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Doctor of Philosophy(PhD),
This thesis describes the synthesis of terminal and internal amino and amidoalkynes and their hydroamination (cyclisation) catalysed by the complex (bis(N-methylimidazol-2-yl)methane)dicarbonylrhodium(I) tetraphenylborate (1). A series of analogous palladium complexes were also prepared and investigated for catalytic hydroamination. The scope of the rhodium(I) complex (1) for the intramolecular hydroamination of more complex amino and amidoalkyne substrates was investigated. This was made possible with the synthesis of aliphatic substrates, namely, 4 pentyn 1 amide (3) and 5 hexyn 1 amide (4) and a number of aromatic substrates, namely, 1, 4 diamino-2, 5 diethynylbenzene (5), 1, 4-diamino-2, 5 bis(phenylethynyl)benzene (6), 2, 3-diamino-1, 4-diethynylbenzene (7), 2, 3-diamino-1, 4-bis(phenylethynyl)benzene (8), 1, 5-bis(acetamido)-2, 4-diethynylbenzene (9), N-(acetyl)-2-ethynylbenzylamine (10) and N-(acetyl)-2-(phenylethynyl)benzylamine (11). The rhodium(I) complex (1) catalytically cyclised the aliphatic 4 pentyn 1 amide (3) regioselectively to the 6 membered ring, 3, 4 dihydro 2 pyridone (64) as the sole product. Attempts to cyclise 5 hexyn 1 amide (4) to produce either the 6 or 7 membered ring were unsuccessful. Compounds 5, 6, 7 and 8 were doubly cyclised to 1, 5 dihydro pyrrolo[2, 3 f]indole (71), 1, 5-dihydro-2, 6-diphenyl-pyrrolo[2, 3 f]indole (73), 1, 8-dihydro-pyrrolo[2, 3 g]indole (74) and 1, 8-dihydro-2, 7-diphenyl-pyrrolo[2, 3 g]indole (75) respectively. The aromatic amides with terminal acetylenes 9 and 10 cyclised to give 1, 7 diacetyl pyrrolo[3, 2 f]indole (76) and N (acetyl) 1, 2 dihydroisoquinoline (77) respectively. However, attempts to cyclise 11 were unsuccessful. Thus the rhodium(I) complex (1) successfully catalysed via hydroamination both terminal and internal acetylenic amine and amide substrates, to give pyridones, indoles and isoquinolines. Cationic and neutral palladium complexes incorporating the bidentate heterocyclic nitrogen donor ligand bis(N-methylimidazol-2-yl)methane (bim; 2) were synthesised: [Pd(bim)Cl2] (15), [Pd(bim)2][BF4]2 (17) [Pd(bim)(Cl)(CH3)] (14), [Pd(bim)(CH3)(NCCH3)][BF4] (16). All of the complexes were active as catalysts for the intramolecular hydroamination reaction, using the cyclisation of 4 pentyn 1 amine (21) to 2 methyl 1 pyrroline (22) as the model test reaction. Percentage conversions, turnover numbers and reaction profiles for each complex were compared to the rhodium(I) complex (1). These studies have shown that the catalytic activity was not significantly dependent on the bim donor ligand or the choice of metal. Substitution of the bim (2) ligand with the COD ligand and the use of methanol as the solvent did impact significantly on the efficiency of the hydroamination reactions.
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2

Shasha, Adelle. "Metal-Catalysed Hydroamination." Thesis, The University of Sydney, 2006. http://hdl.handle.net/2123/1710.

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This thesis describes the synthesis of terminal and internal amino and amidoalkynes and their hydroamination (cyclisation) catalysed by the complex (bis(N-methylimidazol-2-yl)methane)dicarbonylrhodium(I) tetraphenylborate (1). A series of analogous palladium complexes were also prepared and investigated for catalytic hydroamination. The scope of the rhodium(I) complex (1) for the intramolecular hydroamination of more complex amino and amidoalkyne substrates was investigated. This was made possible with the synthesis of aliphatic substrates, namely, 4 pentyn 1 amide (3) and 5 hexyn 1 amide (4) and a number of aromatic substrates, namely, 1, 4 diamino-2, 5 diethynylbenzene (5), 1, 4-diamino-2, 5 bis(phenylethynyl)benzene (6), 2, 3-diamino-1, 4-diethynylbenzene (7), 2, 3-diamino-1, 4-bis(phenylethynyl)benzene (8), 1, 5-bis(acetamido)-2, 4-diethynylbenzene (9), N-(acetyl)-2-ethynylbenzylamine (10) and N-(acetyl)-2-(phenylethynyl)benzylamine (11). The rhodium(I) complex (1) catalytically cyclised the aliphatic 4 pentyn 1 amide (3) regioselectively to the 6 membered ring, 3, 4 dihydro 2 pyridone (64) as the sole product. Attempts to cyclise 5 hexyn 1 amide (4) to produce either the 6 or 7 membered ring were unsuccessful. Compounds 5, 6, 7 and 8 were doubly cyclised to 1, 5 dihydro pyrrolo[2, 3 f]indole (71), 1, 5-dihydro-2, 6-diphenyl-pyrrolo[2, 3 f]indole (73), 1, 8-dihydro-pyrrolo[2, 3 g]indole (74) and 1, 8-dihydro-2, 7-diphenyl-pyrrolo[2, 3 g]indole (75) respectively. The aromatic amides with terminal acetylenes 9 and 10 cyclised to give 1, 7 diacetyl pyrrolo[3, 2 f]indole (76) and N (acetyl) 1, 2 dihydroisoquinoline (77) respectively. However, attempts to cyclise 11 were unsuccessful. Thus the rhodium(I) complex (1) successfully catalysed via hydroamination both terminal and internal acetylenic amine and amide substrates, to give pyridones, indoles and isoquinolines. Cationic and neutral palladium complexes incorporating the bidentate heterocyclic nitrogen donor ligand bis(N-methylimidazol-2-yl)methane (bim; 2) were synthesised: [Pd(bim)Cl2] (15), [Pd(bim)2][BF4]2 (17) [Pd(bim)(Cl)(CH3)] (14), [Pd(bim)(CH3)(NCCH3)][BF4] (16). All of the complexes were active as catalysts for the intramolecular hydroamination reaction, using the cyclisation of 4 pentyn 1 amine (21) to 2 methyl 1 pyrroline (22) as the model test reaction. Percentage conversions, turnover numbers and reaction profiles for each complex were compared to the rhodium(I) complex (1). These studies have shown that the catalytic activity was not significantly dependent on the bim donor ligand or the choice of metal. Substitution of the bim (2) ligand with the COD ligand and the use of methanol as the solvent did impact significantly on the efficiency of the hydroamination reactions.
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Book chapters on the topic "Terminal and internal amino and amidoalkynes"

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Wadsworth, Cynthia L., Mark W. Knuth, Laura W. Burrus, Bradley B. Olwin, and Ronald L. Niece. "Reusing PVDF Electroblotted Protein Samples After N-Terminal Sequencing To Obtain Unique Internal Amino Acid Sequence." In Techniques in Protein Chemistry III, 61–68. Elsevier, 1992. http://dx.doi.org/10.1016/b978-0-12-058756-8.50012-2.

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Taber, Douglass F. "Alkaloid Synthesis: (+)-Preussin (Britton), (±)-Xenovenine (Livinghouse), (+)-Subincanadine F (Li), (±)-Strychnine (Reissig),(-)-Virginiamycin M2 (Panek)." In Organic Synthesis. Oxford University Press, 2013. http://dx.doi.org/10.1093/oso/9780199965724.003.0059.

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Aldehydes such as 1 are readily available by direct enantioselective chlorination. Robert Britton of Simon Fraser University found (Org. Lett. 2010, 12, 4034) that the addition of the kinetic ketone enolate 2 gave the anti aldol 3. Condensation of the chlorohydrin 3 with a primary amine led to the cyclic pyrrolinium salt, that was reduced with high diastereocontrol to (+)-preussin 4. Tom Livinghouse of Montana State University developed Sc catalysts for the cyclization of γ-amino terminal alkenes such as 5. In contrast, addition to internal alkenes was sluggish. He has now shown (Org. Lett. 2010, 12, 4271) that a thiophene substituent activated the internal alkene for addition, enabling the facile synthesis of (±)-xenovenine 7. Chaozhong Li of the Shanghai Institute of Organic Chemistry found (Chem. Commun. 2010, 46, 8436) that ferrocenium ion cleanly oxidized the enolate of the β-keto ester 8, effecting cyclization to 9. The D-tryptophan-derived ester that directed the relative and absolute configuration of the cyclization could readily by removed, delivering (+)-subincanadine F 10. In a complementary approach to indole alkaloid synthesis, Hans-Ulrich Reissig of the Freie Universität Berlin devised (Angew. Chem. Int. Ed. 2010, 49, 8021) the elegant SmI2 -mediated double cyclization of 11 to 12. This set the stage for the assembly of (±)-strychnine 13. James S. Panek of Boston University used (Angew. Chem. Int. Ed. 2010, 49, 6165) the enantiomerically pure allylic silanes that he has developed to construct the chloroaldehyde 14. He found that the reductive cyclization to 15 was best carried out with SmI2 in benzene. SmI2 has the virtue that it is soluble in common organic solvents, so it can readily be deployed even on a micromolar scale. It is also versatile, because its reducing power can be tuned by the solvent in which it is dissolved.
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