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.

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 Core提供的研究能力帮助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非常宝贵的。然而，一级结构只是理解蛋白质功能机制所需的完整结构特征的一部分。还必须知道三维(3D)结构。在最初的结构-功能研究中，蛋白质的片段/结构域可以通过固相多肽合成来有效地合成。这些片段可能是结构、功能结构域或用于提高抗体的表位。片段/结构域的选择通过使用结构生物信息学工具来完成。利用手性光谱(ECD和VCD)在溶液中对蛋白质、蛋白质片段和合成多肽进行了三维结构表征。这些方法虽然分辨率低，但提供了初始结构信息，并有助于其他高分辨率技术确定更精细的结构。ECD和VCD光谱的结构进一步用分子动力学(MD)模拟来表征，以揭示精细的结构细节和结构的稳定性。此外，同源建模和分子对接结合分子动力学模拟被用来设计多肽和蛋白质相互作用结构域的功能类似物。