Urry D W, Long M M, Sugano H
J Biol Chem. 1978 Sep 25;253(18):6301-2.
The cyclic dodecapeptide analog of the linear polyhexapeptide of tropoelastin crystallizes from water on raising of the temperature and thereby demonstrates an inverse temperature transition implying dominant intermolecular hydrophobic interactions. The temperature profiles of turbidity (TP tau) of the cyclododecapeptide are analogous to those of the polyhexapeptide where increases in concentration lead to translations of the profiles to lower temperature without sharpening of the transition. The demonstration of increase in order with increase in temperature for the cyclododecapeptide in water and the similarity of TPtau's lends credence to the view that increases in temperature lead to increases in order, specifically, for the linear polyhexapeptide and, generally, for the precursor protein of the elastic fiber wherein the repeating hexapeptide occurs.
原弹性蛋白线性多六肽的环状十二肽类似物在温度升高时从水中结晶，从而表现出逆温度转变，这意味着分子间疏水相互作用占主导。环十二肽的浊度温度曲线（TP tau）与多六肽的类似，浓度增加会导致曲线向低温平移，而转变不会变尖锐。环十二肽在水中随温度升高有序度增加的证明以及TPtau的相似性，支持了这样一种观点，即温度升高会导致有序度增加，具体而言，对于线性多六肽，一般而言，对于其中存在重复六肽的弹性纤维前体蛋白也是如此。
