CUMC: PROTEOMICS

CUMC：蛋白质组学

• 批准号: 8359992
• 负责人: Sandor Lovas
• 金额: $ 10.52万
• 依托单位: UNIVERSITY OF NEBRASKA MEDICAL CENTER
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-05-01 至 2012-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8359992
• 关键词: Antibodies; Bioinformatics; Biological; Complement; Docking; Epitopes; Funding; Grant; Homology Modeling; Methodology; National Center for Research Resources; Nebraska; Peptide Synthesis; Phase; Principal Investigator; Protein Fragment; Proteins; Research; Research Infrastructure; Research Personnel; Resolution; Resources; SHFM1 gene; Sequence Homology; Solid; Solutions; Source; Spectrum Analysis; Structure; Techniques; Tertiary Protein Structure; United States National Institutes of Health; analog; cost; design; functional genomics; 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

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