U.S.-Spain Cooperative Research: Studies of Interface-Folding-Energetics Relationship in Protein Fragment Recognition

美国-西班牙合作研究：蛋白质片段识别中的界面-折叠-能量学关系研究

• 批准号: 0072029
• 负责人: Maria Luisa Tasayco
• 金额: $ 1.86万
• 依托单位: CUNY City College
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-08-01 至 2003-07-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=0072029&HistoricalAwards=false
• 关键词: U.S.; Spain; Cooperative; Research; Studies

0072029TasaycoThis three-year award, which supports U.S. Spain cooperative research in molecular biology, involves Maria Tasayco of the City University of New York's City College and Jose Sanchez-Ruiz of the University of Granada and Angeles Jimenez of the Center for the Structure of Materials in Madrid, Spain. The objective of their research is to map out which regions from a family of complementary protein fragments are essential for their reassembly. Specifically, they will change the interface surface between folded complementary fragments while maintaining the overall architecture to produce a flat or intertwined interface with the Thioredoxin (Trx) model system. They will clarify how the interface affects the stability and the rate constant of dissociation/unfolding of the artificially generated heterodimers derived from Trx. The U. S. investigator brings to this collaboration expertise in designing, engineering, and generating protein fragments and conducting kinetic studies of folding/binding processes between protein fragments. This is complemented by the Spanish investigators' strengths in thermodynamic studies of protein folding and stability using calorimetry, and in NMR studies of proteins, protein fragments and their complexes. The research will advance our understanding of protein interactions occurring within living organisms and to design ways to modulate the affinity and specificity in protein folding/binding.

这个为期三年的奖项，支持美国和西班牙在分子生物学方面的合作研究，参与者包括纽约城市大学城市学院的Maria Tasayco、格拉纳达大学的Jose Sanchez-Ruiz和西班牙马德里材料结构中心的Angeles Jimenez。他们研究的目的是绘制出互补蛋白片段家族中哪些区域对它们的重组至关重要。具体来说，它们将改变折叠互补片段之间的界面表面，同时保持整体结构，从而与硫氧还蛋白（Trx）模型系统产生平坦或缠绕的界面。他们将阐明界面如何影响由Trx衍生的人工生成的异源二聚体的稳定性和解离/展开的速率常数。这位美国研究者为这次合作带来了设计、工程和生成蛋白质片段的专业知识，并对蛋白质片段之间的折叠/结合过程进行动力学研究。西班牙研究人员在利用量热法研究蛋白质折叠和稳定性的热力学方面的优势，以及在蛋白质、蛋白质片段及其复合物的核磁共振研究方面的优势，补充了这一点。这项研究将促进我们对生物体内发生的蛋白质相互作用的理解，并设计出调节蛋白质折叠/结合的亲和力和特异性的方法。