Structures of polypeptides from α-amino acids disubstituted at the α-carbon
Structures of polypeptides from α-amino acids disubstituted at the α-carbon
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α-碳二取代的α-氨基酸的多肽结构
DOI：
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发表时间：
1991
期刊：
影响因子：
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通讯作者：
E. Benedetti
中科院分区：
文献类型：
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作者：
C. Toniolo;E. Benedetti
通过构象能计算、X-射线衍射分析和波谱研究，对α-氨基异丁酸、DIG(C-α，α-二乙基甘氨酸)、DPG(C-α，α-二丙基甘氨酸)和Ac-c(1-氨基环烷-1-羧酸；n=3，5，6)残基的结构择优进行了综述。结果表明，这些C-α，α-二取代的α-氨基酸残基的长序列优先采用310-螺旋和完全延伸的(C5)构象，这取决于它们侧链的体积和性质(无论是线性的还是环状的
The structural preferences of homopeptides from Aib(α-aminoisobutyric acid), Deg(Cα , α-diethylglycine), Dpg(Cα , α-dipropylglycine) and Ac n c(1-aminocycloalkane-1-carboxylic acid; n=3,5,6) residues, as determined by conformational energy computations, X-ray diffraction analyses, and spectroscopic studies, are reviewed. The results obtained indicate that the 3 10 -helix and the fully extended (C 5 ) conformation are preferentially adopted by long sequences of these Cα , α-disubstituted α-amino acid residues, depending upon bulkiness and nature (whether linear or cyclic) of their side chains