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的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 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。 基因组测序项目提供了大量的新信息，这些信息对于识别和表征基因产物非常宝贵。 然而，一级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。 对于最初的结构-功能研究，可以使用固相肽合成来有效地合成蛋白质的片段/结构域。 这些片段可以是用于产生抗体的结构域、功能域或表位。 通过使用结构生物信息学工具进行片段/结构域的选择。 蛋白质、蛋白质片段和合成多肽的3D结构表征使用手性光谱（ECD和VCD）在溶液中完成。 这些方法，虽然在低分辨率，提供了初步的结构信息，并帮助其他高分辨率技术，以确定更精细的结构。 用ECD和VCD光谱得到的结构进一步用分子动力学（MD）模拟表征，以揭示精细的结构细节和结构稳定性。 此外，同源建模和分子对接补充MD模拟用于设计多肽和蛋白质的相互作用结构域的功能类似物。