CAPPING INTERACTIONS AND HELIX STABILIZATION

该研究有助于解决折叠问题， 从氨基酸预测蛋白质的空间结构 其多肽链的序列。 在尊重的幅度 折叠问题，这个项目认为预测一个共同的 空间蛋白质亚结构，O '-螺旋。拟议的研究将 研究侧链/多肽骨架氢的贡献 螺旋末端区域的键合相互作用（帽化）， 两者都终止并稳定螺旋结构。 的影响 系统性氨基酸残基置换对螺旋含量的影响 将使用圆二色性和NMR评价模型肽 测量. 这些影响-表示为AA G值，将 引入当代算法，用于预测螺旋 结构

This research contributes to the solution of the folding problem, the prediction of the spatial structure of a protein from the amino acid sequence of its polypeptide chain. In deference to the magnitude of the folding problem, this project considers the prediction of a common spatial protein substructure, the o'-helix. The proposed research will investigate the contribution of side-chain/polypeptide backbone hydrogen bonding interactions (capping) in the terminal regions of a helix which both terminate and stabilize the helical structure. The effect of systematic amino acid residue replacements on the helical content of model peptides will be evaluated using both circular dichroism and NMR measurements. These effects- expressed as AA G values, will be introduced into contemporary algorithms for prediction of helical structure.