UNDERSTANDING B SHEET STRUCTURE IN AQUEOUS SOLUTION

了解水溶液中的 B 片结构

• 批准号: 6180374
• 负责人: JEFFERY W KELLY
• 金额: $ 22.23万
• 依托单位: SCRIPPS RESEARCH INSTITUTE, THE
• 依托单位国家: 美国
• 财政年份: 1994
• 资助国家: 美国
• 起止时间: 1994-09-01 至 2002-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6180374
• 关键词: analytical ultracentrifugation; chemical models; circular dichroism; hydrogen bond; infrared spectrometry; interferometry; mass spectrometry; model design /development; nuclear magnetic resonance spectroscopy; peptide chemical synthesis; protein structure; synthetic peptide; thermodynamics; water solution

DESCRIPTION: This is a competitive renewal request for continuation of a program of studies aimed at understanding the chemical principals governing the folding, stability and self-association of beta-sheet structures in aqueous solution. Three lines of investigation are proposed: 1) the design and synthesis of templates that can be inserted into sequences to facilitate sheet formation and to determine of what kind of amino acids are thermodynamically favored to form sheets, and the role of hydrophobic clusters and hydrogen bonds in driving sheet formation; 2) studies of a naturally occurring 38-residue, 3-stranded antiparallel beta-sheet domain (termed the WW domain because of its 2 Trp residues) aimed at understanding the interactions that stabilize the domain structure; 3) studies of intermolecular beta-sheet formation using hosts that can selectively bind peptides. The peptides are obtained by solid phase chemical synthesis, and in the case of the WW domain, using a bacterial expression system. The peptide structures are evaluated by analytical ultracentrifugation, CD, FTIR, NMR, mass spectroscopy, binding of hydrophobic probes (ANS), fluorescence, as well as sequence analysis, in the case of the WW domain motif that has been identified in a number of proteins.

这是一份竞争性续期申请