Probing Natively Disordered Proteins with Selective Noncovalent Adduct Protein Pr

用选择性非共价加合物蛋白 Pr 探测天然无序蛋白

• 批准号: 7945317
• 负责人: Ryan Roy Julian
• 金额: $ 28.51万
• 依托单位: UNIVERSITY OF CALIFORNIA RIVERSIDE
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-09-30 至 2012-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7945317
• 关键词: Affect; Alzheimer' s Disease; Amino Acids; Behavior; Binding; Biological Models; Brain Chemistry; Charge; Chemicals; Disease; Equilibrium; Evaluation; Goals; Health; Human; Ions; Link; Malignant Neoplasms; Mass Spectrum Analysis; Membrane Proteins; Metals; Methodology; Methods; Molecular; Molecular Conformation; Multiple Partners; Mutation; Neurodegenerative Disorders; Neurons; Parkinson Disease; Pathology; Play; Point Mutation; Population; Predisposition; Process; Property; Protein Dynamics; Proteins; Research; Research Personnel; Role; Sampling; Sequence Homology; Side; Structure; Synuclein Family; Techniques; Testing; Ubiquitin; Variant; Vertebral column; Work; adduct; alpha synuclein; design; ionization; ionization technique; metal poisoning; mutant; nervous system disorder; protein aggregation; protein folding; protein function; protein structure; research study; synuclein; tool

The proposed research will develop new methodologies utilizing mass spectrometry for examining protein structure, which is the key to understanding protein function and critical for a molecular level understanding of virtually every disease. This research will enable facile new experiments for studying protein folding and verifying native protein folds, etc... Particular emphasis will be placed on examination of natively unfolded proteins, a reclusive class of molecules related to many neurological diseases and cancer. These goals will be achieved by experiments utilizing noncovalent mass tags designed to respond to the chemical availability of select amino acid side chains on protein surfaces. By facilitating access to protein structure via simple yet sensitive experiments which can be carried out in less than a day, human health will be benefited in diverse ways. More specifically, this technique will be used to study the mechanism by which alpha-synuclein improper aggregates which is implicated in diseases such as Parkinson's and Alzheimer's.

拟议的研究将开发利用质谱的新方法 用于检查蛋白质结构，这是理解蛋白质功能的关键 对于从分子水平理解几乎所有疾病都至关重要。这 研究将使研究蛋白质折叠和验证的新实验变得容易 天然蛋白质折叠等...特别重点将放在检查 天然未折叠的蛋白质，一类与许多相关的隐匿分子 神经系统疾病和癌症。这些目标将通过实验来实现 利用旨在响应化学可用性的非共价质量标签 选择蛋白质表面的氨基酸侧链。通过促进蛋白质的获取 通过简单而灵敏的实验来构建结构，这些实验可以在不到 有一天，人类健康将以多种方式受益。更具体地说，该技术 将用于研究α-突触核蛋白不适当聚集的机制 它与帕金森氏症和阿尔茨海默氏症等疾病有关。