瞬时和异质蛋白质复合物的结构表征-猫眼课题宝

瞬时和异质蛋白质复合物的结构表征

批准号：

8895472

负责人：

Nozomi Ando

金额：

$24.9万

依托单位：

PRINCETON UNIVERSITY

依托单位国家：

美国

项目类别：

财政年份：

2012

资助国家：

美国

项目状态：

已结题

起止时间：

2012-02-02 至 2017-07-31

来源：

https://reporter.nih.gov/project-details/8895472

关键词：

Allosteric Regulation Amino Acids Antineoplastic Agents Arakawa syndrome 2 Behavior Biochemical Biological Process Biology Cell Cycle Cells Chemicals Complement Complex Congenital Abnormality Crystallization Crystallography DNA biosynthesis Data Deoxyribonucleotides Disease Drug Design Drug Targeting Effectiveness Enzymes Escherichia coli Funding Gene Mutation Goals Heart Human Individual Investigation Kinetics Learning Link Malignant Neoplasms Megaloblastic Anemia Mentors Metabolism Methionine Methods Modeling Molecular Biology Molecular Conformation Nature Neural tube Nucleotides Organism Pharmaceutical Preparations Phase Physiological Play Pregnancy Protein Isoforms Proteins Public Health Regulation Research Ribonucleotide Reductase Roentgen Rays Role S-Adenosylmethionine Sampling Solutions Spectrum Analysis Structure System Time Training Vitamin B 12 Work analytical ultracentrifugation base flexibility in vivo insight mathematical methods meetings prevent protein complex

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中文摘要

翻译

瞬时和异相蛋白质相互作用在催化和调节过程中都发挥着重要作用。蛋白质复合体和多模块机械的功能。然而，涉及到的技术挑战此类系统的结构特征为理解其内在特性设置了关键障碍行为。依赖维生素B12的蛋氨酸合成酶和Ia类核苷酸还原酶是两种这些酶是这类系统的缩影，在这些系统中，对其多重构象的结构洞察将取得进展我们对它们的生理和医学相关行为的理解。迎接技术挑战在研究这些系统时，我将利用通过Small-And获得的整体结构信息广角X射线散射，并使用数学方法将混合物解卷为可量化的个别州。这项工作将得到结晶学、光谱学和分析的补充。超速离心法。

英文摘要

Transient and heterogeneous protein interactions play important roles both in the catalytic and regulatory functions of protein complexes and multi-modular machinery. However, the technical challenges involved in structural characterizations of such systems have placed critical barriers against understanding their intrinsic behavior. The vitamin B12-dependent methionine synthase and class Ia ribonucleotide reductases are two enzymes that epitomize such systems where structural insight into their multiple conformations will advance our understanding of their physiological and medically relevant behavior. To meet the technical challenge of investigating these systems, I will exploit the ensemble structural information that can be gained by small- and wide-angle X-ray scattering and employ mathematical methods to deconvolute the mixtures into quantifiable individual states. This work will be complemented by crystallography, spectroscopy, and analytical ultracentrifugation.

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