AMIDE-TO-ESTER MUTATIONS IN INVESTIGATING FOLDING OF HELICAL PROTEINS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 骨架-骨架氢键(H键)是天然蛋白质结构的常见和重要特征，但它们在折叠过渡态结构中的作用尚不清楚。一种可能性是H-键是在折叠过程中形成天然侧链接触的结果。另一种可能性是，它们通过提供一个框架，引导折叠流向原生状态，从而发挥更具决定性的作用。为了更好地了解骨架-骨架氢键在蛋白质折叠中的动力学影响，我们使用phi值分析方法结合酰胺到酯(A-to-E)骨架突变，研究了螺旋氢键在Villin头饰亚域(HP-35)折叠动力学中的作用。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Backbone-backbone hydrogen bonds (H-bond) are common and apparently important features of native protein structures, yet their role in folding transition state structure remains unclear. One possibility is that H-bonds result as a consequence of the formation of native sidechain contacts during folding. Another possibility is that they play a more deciding role by providing a framework that directs the flow of folding toward the native state. To provide a better understanding of the kinetic influence of backbone-backbone H-bonds in protein folding, we investigate the role of helical H-bonding in the folding kinetics of the villin headpiece subdomain (HP-35) using the Phi-value analysis method in conjunction with amide-to-ester (A-to-E) backbone mutagenesis.