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INVESTIGATIONS OF MACROMOLECULAR STRUCTURES AND DYNAMICS IN SOLUTION BY NMR

INVESTIGATIONS OF MACROMOLECULAR STRUCTURES AND DYNAMICS IN SOLUTION BY NMR
通过核磁共振研究溶液中的大分子结构和动力学
批准号:
6432093
负责人:
ANGELA M. GRONENBORN
金额:
$0.0万
依托单位国家:
美国
项目类别:
财政年份:
--
资助国家:
美国
项目状态:
未结题
起止时间:
至

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中文摘要
翻译
该实验室的总体研究目标集中在尽可能完整地描述肽,蛋白质,核酸及其复合物在溶液中的结构,主要是通过NMR光谱。 目前,特别强调的是发展的方法,使调查更大和复杂的系统,以及增加精度,这些解决方案的结构可以得到。进行了旨在关联结构和功能的研究以及旨在研究蛋白质折叠的实验。已经对几种蛋白质进行了结构研究。这些HIV-1蛋白酶,氰威蛋白-N,GB 1及其突变体。 此外,还对一些蛋白质核酸复合物进行了研究,包括野生型SRY和该蛋白质的性别逆转突变体以及转录激活因子MarA的蛋白质核酸复合物。开发了用于在磁场中部分排列分子的新介质,其特征在于并用于测量残余偶极耦合。
英文摘要
The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained. Studies aimed at correlating structure and function, and experiments aimed at investigating protein folding are conducted. Structural studies for several proteins have been carried out. These HIV-1 protease, cyanovirin-N, GB1 and mutants thereof. In addition, work was also carried out on a number of protein nucleic acid complexes, including those of the wild-type SRY and a sex-reversal mutant of this protein and the transcriptional activator MarA. New media for partially aligning molecules in the magnetic field were developed, characterized and exploited for measuring residual dipolar couplings.
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Molecular, Cellular and Behavioral Impact of the R203W PACS1 Syndrome Mutation
Administrative Core
Pittsburgh Center for HIV Protein Interactions (PCHPI)
Pittsburgh Center for HIV Protein Interactions (PCHPI)
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