FORCE FIELD EFFECTS ON THE SOLUTION STRUCTURE OF MELITTIN AND N-FORMYL MELITTIN

力场对蜂毒素和N-甲酰蜂毒素溶液结构的影响

• 批准号: 7601521
• 负责人: JEFFREY WOLBACH
• 金额: $ 0.03万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-08-01 至 2008-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601521
• 关键词: Amino Acids; Charge; Computer Retrieval of Information on Scientific Projects Database; Funding; Grant; Hemolysis; Institution; Organism; Peptides; Play; Research; Research Personnel; Resources; Role; Solutions; Source; Structure; Thinking; United States National Institutes of Health; Venoms; peptide structure

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 26-amino acid peptide melittin is a primary component of honeybee venom, and is produced in two forms by the organism: a form with a charged N-terminus (NH3+) and a form where the N-terminus is formylated. Melittin is highly helical and it is thought that the peptide secondary structure plays a key role in melittins ability to participate in hemolysis. This study is undertaken to understand whether the N-formylation has a profound effect on the solution secondary structure of the peptide, and whether the observed differences in secondary structure are force-field dependent.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 26-氨基酸肽融合素是蜜蜂毒液的主要成分，由生物体以两种形式产生：一种带有带电的N末端（NH3+）的形式，是N-末端被打印的形式。蜂毒素是高度螺旋的，人们认为肽二级结构在参与溶血的能力中起关键作用。这项研究是为了了解N-甲基化是否对肽的溶液二级结构以及观察到的二级结构差异是否具有力场依赖性。