BETA HAIRPINS OF BRAZZEIN TERMINI

BRAZZEIN TERMINI 的 Beta 发夹

• 批准号: 8361255
• 负责人: FARIBA M ASSADI-PORTER
• 金额: $ 0.2万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361255
• 关键词: Funding; Grant; Human; Modeling; Mutagenesis; National Center for Research Resources; Peptides; Principal Investigator; Research; Research Infrastructure; Resources; Side; Site; Source; United States National Institutes of Health; beta pleated sheet; cost; design; receptor; sweet taste perception

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Combined mutagenesis and modeling results suggest that the termini of brazzein may be the primary brazzein-side interaction site between brazzein and the human sweet taste receptor. The termini of brazzein are involved in an antiparallel beta-sheet, which has allowed us to design beta-hairpin peptides derived from the termini. If the the termini are indeed the primary site of interaction, these peptides derived from the terminal motifs should show at least minimal activity.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， NCRR赠款不直接向子项目或子项目工作人员提供资金。 结合诱变和建模的结果表明，末端的甜味蛋白可能是主要的甜味蛋白与人类甜味受体之间的相互作用位点。植物甜蛋白的末端参与了一个反向平行的β折叠，这使得我们能够设计来自末端的β-发夹肽。如果末端确实是相互作用的主要位点，则衍生自末端基序的这些肽应显示至少最小的活性。