Conformational preferences of oligopeptides rich in alpha-aminoisobutyric acid. I. Observation of a 3(10)/alpha-helical transition upon sequence permutation.
Conformational preferences of oligopeptides rich in alpha-aminoisobutyric acid. I. Observation of a 3(10)/alpha-helical transition upon sequence permutation.
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富含α-氨基异丁酸的寡肽的构象偏好。
DOI：
10.1002/bip.360311410
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发表时间：
1991
期刊：
影响因子：
2.9
通讯作者：
Kuki,A
中科院分区：
文献类型：
--
作者：
Basu,G;Bagchi,K;Kuki,A
富含α，α-二烷基化氨基酸Aib的肽的溶液构象已被证明是一个微妙的问题，不是因为螺旋/卷曲转变，而是因为α-螺旋/310-螺旋竞争。已经合成了一系列含有75% Aib的特殊肽，其具有相同的氨基酸组成但不同的序列;它们是序列排列异构体。核磁共振氢键研究表明，在该集合内的两种替代螺旋形式之间存在序列排列诱导的转变。的螺旋Aib-丰富的肽的设计和构象预测的影响进行了讨论。
The solution conformation of peptides rich in the α,α‐dialkylated amino acid Aib has proven to be a subtle problem, not because of helix/coil transitions, but rather because of α‐helical/310‐helical competition. A special series of peptides containing 75% Aib has been synthesized that feature identical amino acid composition but differing sequences; they are sequence permutation isomers. Nuclear magnetic resonance hydrogen‐bonding studies reveal that there is a sequence permutation induced transition between the two alternative helical forms within this set. The implications for the design and conformational prediction of helical Aib‐rich peptides are discussed.