Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.
Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.
复制标题
通过可变温度圆形二色性和等温滴定量热法对二级结构和自组装的分析。
DOI：
10.1002/prot.22369
复制
发表时间：
2009-08-15
影响因子：
2.9
通讯作者：
Moradian-Oldak, Janet
中科院分区：
文献类型：
--
作者：
Lakshminarayanan, Rajamani;Yoon, Il;Hegde, Balachandra G.;Fan, Daming;Du, Chang;Moradian-Oldak, Janet
关键词：
釉原蛋白是一种富含脯氨酸的釉质基质蛋白，在釉质晶体的定向生长过程中起着重要作用。在疏水相互作用的作用下，釉原蛋白自组装形成纳米球和高阶结构。本研究旨在通过计算和生物物理方法更好地了解釉原蛋白的一级-二级结构和自组装之间的关系。变温圆二色谱研究表明，在生理pH条件下，重组猪釉原蛋白含有无序结构，且在较低温度下含有较多的PPII结构。增加rP172的浓度可以促进折叠向有序的β结构的组装。等温滴定热法稀释研究表明，在所有温度下，由于疏水效应，自组装是以熵驱动的，摩尔组装热(ΔHA)随着温度的升高而降低。使用计算方法，已经确定了氨基酸序列中具有高组装倾向和具有PPII结构的结构域的轮廓。我们的结论是，釉原蛋白的组装特性是由于疏水和PPII螺旋倾向区之间的互补所致。
Amelogenin is a proline-rich enamel matrix protein known to play an important role in the oriented growth of enamel crystals. Amelogenin self-assembles to form nanospheres and higher order structures mediated by hydrophobic interactions. This study aims to obtain a better insight into the relationship between primary-secondary structure and self-assembly of amelogenin by applying computational and biophysical methods. Variable temperature circular dichroism studies indicated that under physiological pH recombinant full-length porcine amelogenin contains unordered structures in equilibrium with polyproline type II (PPII) structure, the latter being more populated at lower temperatures. Increasing the concentration of rP172 resulted in the promotion of folding to an ordered β-structured assembly. Isothermal titration calorimetry dilution studies revealed that, at all temperatures, self-assembly is entropically driven due to the hydrophobic effect and the molar heat of assembly (ΔHA) decreases with temperature. Using a computational approach, a profile of domains in the amino acid sequence that have a high propensity to assemble and to have PPII structures has been identified. We conclude that the assembly properties of amelogenin are due to complementarity between the hydrophobic and PPII helix prone regions.
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DOI：
10.1046/j.0014-2956.2001.02614.x
发表时间：
2001-12-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Li, GY;Zhou, P;Yu, TY
通讯作者：
Yu, TY
影响因子：
2.9
作者：
Bienkiewicz, EA;Adkins, JN;Lumb, KJ
通讯作者：
Lumb, KJ
影响因子：
2.7
作者：
GOTO, Y;KOGURE, E;AOBA, T
通讯作者：
AOBA, T
影响因子：
11.4
作者：
Knupp, C;Squire, JM
通讯作者：
Squire, JM
影响因子：
3
作者：
FINCHAM, AG;MORADIANOLDAK, J;SLAVKIN, HC
通讯作者：
SLAVKIN, HC