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H-Phe-Tyr-(pATAT)-NH2的固相合成:来自噬菌体phi X174核蛋白的一个核肽片段。

Solid-phase synthesis of H-Phe-Tyr-(pATAT)-NH2: a nucleopeptide fragment from the nucleoprotein of bacteriophage phi X174.

作者信息

Dreef-Tromp C M, van Dam E M, van den Elst H, van der Marel G A, van Boom J H

机构信息

Gorlaeus Laboratories, Leiden, The Netherlands.

出版信息

Nucleic Acids Res. 1990 Nov 25;18(22):6491-5. doi: 10.1093/nar/18.22.6491.

DOI:10.1093/nar/18.22.6491
PMID:2147473
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC332600/
Abstract

The preparation of the nucleopeptide H-Phe-Tyr-(pATAT)-NH2 could be realized via a solid phase phosphitetriester approach and by using the protected protecting group 2-(tert-butyldiphenylsilyoxymethyl)-benzoyl for the masking of the N6-amino function of deoxyadenosine. The latter protecting group can be removed under mild conditions with fluoride ion.

摘要

核肽H-Phe-Tyr-(pATAT)-NH2的制备可通过固相亚磷酸三酯法实现,并使用保护基团2-(叔丁基二苯基硅氧基甲基)-苯甲酰基来掩蔽脱氧腺苷的N6-氨基功能。后一种保护基团可在温和条件下用氟离子除去。

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本文引用的文献

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Polymer support oligonucleotide synthesis XVIII: use of beta-cyanoethyl-N,N-dialkylamino-/N-morpholino phosphoramidite of deoxynucleosides for the synthesis of DNA fragments simplifying deprotection and isolation of the final product.聚合物载体寡核苷酸合成 XVIII:脱氧核苷的β-氰基乙基-N,N-二烷基氨基-/N-吗啉代亚磷酰胺用于 DNA 片段合成,简化最终产物的脱保护和分离
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Characterization of the DNA-protein complex at the termini of the bacteriophage PRD1 genome.噬菌体PRD1基因组末端DNA-蛋白质复合物的特性分析
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Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies.来自脊髓灰质炎病毒1型衣壳蛋白VP1四个不同区域的合成肽可诱导中和抗体。
Proc Natl Acad Sci U S A. 1985 Feb;82(3):910-4. doi: 10.1073/pnas.82.3.910.
7
Alteration of the ATG start codon of the A protein of bacteriophage phi X174 into an ATT codon yields a viable phage indicating that A protein is not essential for phi X174 reproduction.将噬菌体φX174的A蛋白的ATG起始密码子改变为ATT密码子可产生一种有活力的噬菌体,这表明A蛋白对于φX174的繁殖并非必不可少。
FEBS Lett. 1987 Jun 22;218(1):119-25. doi: 10.1016/0014-5793(87)81030-x.
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Nucleic Acids Res. 1989 Apr 25;17(8):2897-905. doi: 10.1093/nar/17.8.2897.
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Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine.
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