CUMC: PROTEOMICS

CUMC：蛋白质组学

• 批准号: 8167479
• 负责人: Sandor Lovas
• 金额: $ 9.88万
• 依托单位: UNIVERSITY OF NEBRASKA MEDICAL CENTER
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8167479
• 关键词: Antibodies; Bioinformatics; Biological; Complement; Computer Retrieval of Information on Scientific Projects Database; Docking; Epitopes; Funding; Grant; Homology Modeling; Institution; Methodology; Molecular; Peptide Synthesis; Phase; Protein Fragment; Proteins; Proteomics; Research; Research Personnel; Resolution; Resources; SHFM1 gene; Solid; Solutions; Source; Spectrum Analysis; Structure; Techniques; Tertiary Protein Structure; United States National Institutes of Health; analog; design; genome sequencing; molecular dynamics; polypeptide; protein function; three dimensional structure; tool

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The research capability provided by the Core helps investigators to understand structural aspects of biological activities of proteins. The genome sequencing projects are providing vast quantities of new information that is invaluable for identifying and characterizing gene products. However, primary structure is only part of the complete structural characterization required for understanding mechanisms of protein functions. The three-dimensional (3D) structures must also be known. For initial structure-function studies, fragments/domains of proteins can be efficiently synthesized using solid phase peptide synthesis. These fragments could be structural, functional domains or epitopes for raising antibodies. The selection of fragments/domains is done by using structural bioinformatics tools. 3D structural characterizations of proteins, protein fragments and synthetic polypeptides is done in solution using chiroptic spectroscopy (ECD and VCD). These methodologies, although at low resolution, provide the initial structural information and help to other high resolution techniques to determine the finer structure. Structures obtained with ECD and VCD spectroscopy are further characterized with molecular dynamics (MD) simulations to reveal fine structural details and structural stabilities. Furthermore, homology modeling and molecular docking complemented with MD simulations is used to design of functional analogs of interacting domains of polypeptides and proteins.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 核心提供的研究能力有助于研究人员了解蛋白质生物活性的结构方面。 基因组测序项目正在提供大量的新信息，这些信息对于识别和表征基因产品是无价的。 但是，主要结构只是理解蛋白质功能机制所需的完整结构表征的一部分。 还必须知道三维（3D）结构。 对于初始结构功能研究，可以使用固相肽合成有效合成蛋白质的片段/域。 这些片段可以是用于提高抗体的结构，功能域或表位。 片段/域的选择是通过使用结构生物信息学工具来完成的。 蛋白质，蛋白质片段和合成多肽的3D结构特征是在使用chiroptic光谱法（ECD和VCD）的溶液中进行的。 这些方法虽然以低分辨率为基础，但为其他高分辨率技术提供了初始结构信息，以确定较精细的结构。 用ECD和VCD光谱获得的结构通过分子动力学（MD）模拟进一步表征，以揭示精细的结构细节和结构稳定性。 此外，与MD模拟相辅相成的同源模型和分子对接用于设计多肽和蛋白质相互作用结构域的功能类似物。