Helix induction potential of N-terminal α-methyl, α-amino acids

被引：7
作者：
Gobbo, M
Biondi, L
Filira, F
Formaggio, F
Crisma, M
Rocchi, R
Toniolo, C
Broxterman, QB
Kamphuis, J
机构：
[1] Univ Padua, Dept Organ Chem, CNR, Biopolymer Res Ctr, I-35131 Padua, Italy
[2] DSM Res BV, Organ Chem & Biotechnol Sect, NL-6160 MD Geleen, Netherlands
[3] DSM Fine Chem, NL-6401 JH Heerlen, Netherlands
来源：
LETTERS IN PEPTIDE SCIENCE | 1998年 / 5卷 / 2-3期
关键词：
alpha-aminoisobutyric acid peptides; circular dichroism; conformational analysis; isovaline peptides; C-peptide;
D O I：
10.1023/A:1008873910529
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A series of longer analogues of the C-peptide of RNAse A has been synthesized with the aim of assessing the helix induction potential in water of alpha-methyl, alpha-amino acids at the N-terminus of the chain. The circular dichroism data indicate that one isovaline residue is effective in increasing the helix content of the 13-residue peptide by about 7%.
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收藏
页码：105 / 107
页数：3
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