M Doi, T Ishida, A Polese, F Formaggio, M Crisma, C Toniolo, Q B Broxterman, J Kamphuis
{"title":"(S)-C α -乙基，C α -苄基甘氨酸[(S)-(α Et)Phe]多肽以左旋螺旋结构折叠。","authors":"M Doi, T Ishida, A Polese, F Formaggio, M Crisma, C Toniolo, Q B Broxterman, J Kamphuis","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The first x-ray diffraction structure analysis of a C alpha-ethyl, C alpha-benzylglycine [(alpha Et)Phe]-containing peptide, N alpha-benzyloxycarbonyl-alpha-aminoisobutyryl-alpha-amino-isobutyr yl-(S)- C alpha-benzylglycyl-alpha-aminoisobutyric acid (methanol solvate), has been performed. In the crystal state the N alpha-protected tetrapeptide is folded in an incipient, left-handed 3(10)-helical structure. This finding confirms that the relationship between (alpha Et)Phe alpha-carbon chirality and screw sense of the helix that is formed is opposite to that exhibited by protein amino acids, including Phe.</p>","PeriodicalId":20005,"journal":{"name":"Peptide research","volume":"8 5","pages":"294-7"},"PeriodicalIF":0.0000,"publicationDate":"1995-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"(S)-C alpha-ethyl, C alpha-benzylglycine [(S)-(alpha Et)Phe] peptides fold in left-handed helical structures.\",\"authors\":\"M Doi, T Ishida, A Polese, F Formaggio, M Crisma, C Toniolo, Q B Broxterman, J Kamphuis\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The first x-ray diffraction structure analysis of a C alpha-ethyl, C alpha-benzylglycine [(alpha Et)Phe]-containing peptide, N alpha-benzyloxycarbonyl-alpha-aminoisobutyryl-alpha-amino-isobutyr yl-(S)- C alpha-benzylglycyl-alpha-aminoisobutyric acid (methanol solvate), has been performed. In the crystal state the N alpha-protected tetrapeptide is folded in an incipient, left-handed 3(10)-helical structure. This finding confirms that the relationship between (alpha Et)Phe alpha-carbon chirality and screw sense of the helix that is formed is opposite to that exhibited by protein amino acids, including Phe.</p>\",\"PeriodicalId\":20005,\"journal\":{\"name\":\"Peptide research\",\"volume\":\"8 5\",\"pages\":\"294-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Peptide research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Peptide research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
首次对含C α -乙基，C α -苄基甘氨酸[(α Et)Phe]- N α -苯氧羰基- α -氨基异丁基- α -氨基异丁基-(S)- C α -苄基甘氨酸- α -氨基异丁酸(甲醇溶剂)肽进行了x射线衍射结构分析。在晶体状态下，受N保护的四肽折叠成一个早期的左旋3(10)螺旋结构。这一发现证实了(α Et)Phe -碳手性与螺旋感之间的关系与所形成的螺旋感与包括Phe在内的蛋白质氨基酸所表现出的相反。
(S)-C alpha-ethyl, C alpha-benzylglycine [(S)-(alpha Et)Phe] peptides fold in left-handed helical structures.
The first x-ray diffraction structure analysis of a C alpha-ethyl, C alpha-benzylglycine [(alpha Et)Phe]-containing peptide, N alpha-benzyloxycarbonyl-alpha-aminoisobutyryl-alpha-amino-isobutyr yl-(S)- C alpha-benzylglycyl-alpha-aminoisobutyric acid (methanol solvate), has been performed. In the crystal state the N alpha-protected tetrapeptide is folded in an incipient, left-handed 3(10)-helical structure. This finding confirms that the relationship between (alpha Et)Phe alpha-carbon chirality and screw sense of the helix that is formed is opposite to that exhibited by protein amino acids, including Phe.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
