Roos H M, van Rooyen P H
Department of Chemistry, University of Pretoria, South Africa.
Int J Pept Protein Res. 1994 Dec;44(6):562-7. doi: 10.1111/j.1399-3011.1994.tb01145.x.
The conformational space of six tetrapeptides from the beta-bends in the third loop of short-chain snake venom neurotoxins was investigated with the aid of energy calculations. It was shown that these peptides can be divided into two groups: those with a specific preference for an alpha-helix and those that exist as an ensemble of beta-turn conformations.
借助能量计算研究了短链蛇毒神经毒素第三环中β-转角处六种四肽的构象空间。结果表明，这些肽可分为两组：对α-螺旋有特定偏好的肽和以β-转角构象集合形式存在的肽。
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