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

研究螺旋蛋白折叠中的酰胺到酯突变

• 批准号: 7955451
• 负责人: JEFFERY A KELLEY
• 金额: $ 0.96万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-06-01 至 2010-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955451
• 关键词: Amides; Computer Retrieval of Information on Scientific Projects Database; Esters; Funding; Grant; Hydrogen Bonding; Institution; Kinetics; Laboratories; Methods; Mutagenesis; Mutation; Optics; Play; Process; Proteins; Research; Research Personnel; Resources; Role; Source; Structure; United States National Institutes of Health; Vertebral column; protein folding; protein structure; villin

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.

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