VILLIN HEADPIECE SUBDOMAIN (VHP) STUDY

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。 肌动蛋白结合蛋白Villin在其最末端含有一个紧凑的f-肌动蛋白结合域，称为“头饰”。这个由76个氨基酸组成的绒毛蛋白头盔结构域(VHP)具有高度的热稳定性。头盔中稳定的折叠结构定位于由C-末端35残基形成的亚区。核磁共振研究表明，头盔亚区含有三个短的α-螺旋，这些相同的螺旋存在于完整头盔的相应区域。HP-35是最小的单体多肽，其特征是只由自然存在的氨基酸组成，这些氨基酸自主折叠成独特的耐热结构，没有二硫键或配体结合。它有一个由3个苯丙氨酸组成的疏水核心，但也有两个基团(一个色氨酸和另一个苯丙氨酸)，这两个基团是疏水的，但(出于功能原因)暴露在溶剂中。我们研究了VHP亚域的一个稳定的五氟苯丙氨酸版本的结构。

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. The actin-bundling protein villin contains, at its extreme C terminus, a compact f-actin binding domain called "headpiece". This 76-amino acid villin headpiece domain (VHP) is highly thermostable. The stable folded structure in headpiece is localized to a subdomain formed by the C-terminal 35 residues. NMR studies indicate that the headpiece subdomain contains three short alpha-helices, and that these same helices are present in the corresponding regions of intact headpiece. HP-35 is the smallest monomeric polypeptide characterized consisting of only naturally occurring amino acids that autonomously folds into a unique and thermostable structure without disulfide bonds or ligand binding. It has a hydrophobic core made of 3 phenylalanines, but also has two groups (a tryptophan and another phenylalanine) which are hydrophobic, but are solvent exposed (for functional reasons). We investigate the structure of a stable pentafluorinated phenylalanine version of the VHP subdomain.