Bodkin M J, Goodfellow J M
Department of Crystallography Birkbeck College, University of London, UK.
Biopolymers. 1996 Jul;39(1):43-50. doi: 10.1002/(SICI)1097-0282(199607)39:1%3C43::AID-BIP5%3E3.0.CO;2-V.
The titration of an aqueous solution of a de novo designed peptide with trifluoroethanol (TFE) shows complete helix formation with the addition of only 30% TFE. A molecular simulation of the peptide, in which a single shell of TFE molecules initially surrounds the peptide, reveals preferred sites of solvent interaction. The TFE molecules show greater preference for the hydrophobic compared with hydrophilic side chains. The helix-enhancing ability of TFE in aqueous solution may be rationalized in terms of stabilizing the hydrophobic collapse of apolar side chains of the formed helix.
用三氟乙醇（TFE）滴定新设计的肽的水溶液，结果表明仅加入30%的TFE就可形成完全的螺旋结构。对该肽进行分子模拟，最初有一层TFE分子围绕着肽，模拟结果揭示了溶剂相互作用的优先位点。与亲水性侧链相比，TFE分子对疏水性侧链表现出更大的偏好。TFE在水溶液中的螺旋增强能力可以通过稳定所形成螺旋的非极性侧链的疏水塌缩来解释。
