ASSOCIATION STATES & ENERGETICS OF TRANMEMBRANE PROTEIN

大多数跨膜蛋白都与α-蛋白一起穿过脂双层。 螺旋由20-25个氨基酸残基组成。它们之间的联系 膜上的α-螺旋对细胞的生物学功能很重要。 跨膜蛋白。尽管如此，人们对此知之甚少 影响螺旋-螺旋相互作用的因素和分子的能量学 协会。这项研究将利用小角x射线散射来研究 血糖素A缔合稳定性和能量学的变化 跨膜结构域对序列变异的反应。当这些因素 导致联想稳定是可以理解的，预测 跨膜蛋白的结构特征将得到改善。

Most transmembrane proteins traverse the lipid bilayers with alpha- helices composed of 20-25 amino acid residues. The association of these alpha-helices in membranes is important to the biological functions of transmembrane proteins. In spite of this, little is known about the factors governing the helix-helix interaction and the energetics of association. This study will use small angle x-ray scattering to study the changes in association stability and energetics of glycophorin A transmembrane domain in respond to sequence variations. When the factors leading to association stability can be understood, predictions of structural features of transmembrane proteins will be advanced.