VILLIN HEADPIECE SUBDOMAIN (VHP) STUDY

点击翻译按钮获取中文摘要

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.