RACEMIC PROTEIN CRYSTALLOGRAPHY

外消旋蛋白质晶体学

• 批准号: 8361686
• 负责人: TODD O YEATES
• 金额: $ 0.48万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-04-01 至 2012-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361686
• 关键词: Amino Acids; Anti-Bacterial Agents; Bacillus anthracis; Bacillus megaterium; Biological Assay; Crystallography; Diffusion; Funding; Grant; National Center for Research Resources; Principal Investigator; Proteins; Radial; Research; Research Infrastructure; Resources; Snake Venoms; Source; United States National Institutes of Health; chemical synthesis; cost; enantiomer; structural biology

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. The 50-residue snake venom protein L-omwaprin and its enantiomer D-omwaprin were prepared by total chemical synthesis. Radial diffusion assays were performed against Bacillus megaterium and Bacillus anthracis; both L- and D-omwaprin showed antibacterial activity against B. megaterium. The native protein enantiomer, made of L-amino acids, failed to crystallize readily. However, when a racemic mixture containing equal amounts of L- and D-omwaprin was used, diffraction quality crystals were obtained.

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