CIRCULAR DICHROISM SPECTROPOLARIMETER

圆二色谱(CD)是一种光谱方法，它提供了 关于蛋白质的二级和三级结构的信息 和核酸。CD是一种用于检测分子的光学技术 它们与左、右圆偏振光的相互作用不同。 大多数生物分子是手性的这一事实意味着应用 因为CD在重要大分子的表征中的使用是 很普遍。蛋白质、多肽和核酸在特定的条件下吸收光线 由于分子中的基团，可见和紫外区的区域 叫做生色团。因此，CD可以生成关于辅助服务器的信息 生物大分子的结构和结合 配基到分子上，提供构象变化的证据。 正因为如此，圆二向色性在过去的几年中得到了承认 十年来，生物医学研究人员的广泛基础。在这份提案中， 伯纳姆研究所的调查人员(包括结构生物学家、 细胞生物学家、神经生物学家、糖生物学家、生物化学家和 肿瘤学家)申请资金购买圆二向色性 光谱偏振仪。 伯纳姆研究所(前身为拉霍亚癌症研究基金会) 一家非营利性生物医学研究所和一家NCI癌症中心 由33名主要调查人员组成的工作人员。CD将提供独特的功能 需要推进十几种重要蛋白质的研究或 多肽，包括分析以表征稳定性、完整性和 蛋白质的物理性质，以监测蛋白质复性，以评估 蛋白质-核酸和蛋白质-肽的相互作用，并测试 糖基化对蛋白质结构的影响。CD光谱偏振仪 将作为共享资源运行。一名操作员/经理被 确定哪些人具有丰富的CD使用经验，并将 负责仪器的日常运行。一家内部公司 咨询委员会，由这一事件的首席调查员担任主席 应用，将监督裁谈会的使用和科学产出 光谱偏振仪。

Circular dichroism (CD) is a spectroscopic method that provides information about both the secondary and tertiary structure of proteins and nucleic acids. CD is an optical technique used to detect molecules that interact differently with right and left circularly polarized light. The fact that most biological molecules are chiral means that applications for the use of CD in the characterization of important macromolecules is widespread. Proteins, peptides and nucleic acids absorb light in specific areas of the visible and ultraviolet regions due to groups in the molecule called chromophores. Thus CD can generate information about the secondary structure of biological macromolecules and also about the binding of ligands to the molecules, providing evidence of conformational change. Because of this, circular dichroism has become recognized in the last decade by a broad base of biomedical investigators. In this proposal, investigators at the Burnham Iintitute (including structural biologists, cell biologists, neurobiologists, glycobiologists, biochemists and oncologists) request funding to purchase a circular dichroism spectropolarimeter. The Burnham Institute (formerly La Jolla cancer Research Foundation) is a non-profit biomedical research institute and an NCI Cancer Center with a staff of 33 principal investigators. CD will provide unique capabilities needed to advance the studies of more than a dozen important proteins or peptides, including analyses to characterize stability, integrity and physical properties of proteins, to monitor protein refolding, to evaluate protein-nucleic acid and protein-peptide interactions and to test the effects of glycosylation on protein structure. The CD spectropolarimeter will be operated as a shared resource. An operator/manager has been identified who has significant experience using CD and will take responsibility for the day-to-day operation of the instrument. An internal advisory committee, chaired by the principal investigator of this application, will oversee the utilization and scientific output of the CD spectropolarimeter.