U.S.-France Cooperative Research: Kinetic Studies of the Folding of Thioredoxin By Fragment Complementation

美法合作研究：通过片段互补进行硫氧还蛋白折叠的动力学研究

• 批准号: 9600006
• 负责人: Maria Luisa Tasayco
• 金额: $ 1.8万
• 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: 1996
• 资助国家: 美国
• 起止时间: 1996-06-01 至 1999-05-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9600006&HistoricalAwards=false
• 关键词: U.S.; France; Cooperative; Research; Kinetic

This three-year award, which supports U.S.-France cooperative research in molecular biology, involves Maria Tasayco of the City University of New York's City College and Michel Godlberg and Alain Chaffotte of the Institut Pasteur in Paris, France. The objective of their research is to study the protein folding problem. Specifically, they will investigate pathways by which fragments of E. Coli thioredoxin reconstitute the original structure of macromolecules. Through the study of the function of thioredoxin, they propose to elucidate structure and the protein folding pathway. The U.S. investigator brings to this collaboration expertise in structural studies and approaches. This is complemented by the French investigators' expertise in kinetic studies of protein folding. The research will advance our understanding of the relationship between structure and function in biological macromolecules.

这个为期三年的奖项，支持美国-法国分子生物学合作研究，涉及纽约城市大学城市学院的Maria Tasayco和法国巴黎巴斯德研究所的Michel Godlberg和Alain Chaffotte。 他们的研究目标是研究蛋白质折叠问题。 具体地说，他们将研究E.大肠杆菌硫氧还蛋白可重构大分子的原始结构。 通过研究硫氧还蛋白的功能，他们提出了阐明结构和蛋白质折叠途径。 美国的研究人员带来了结构研究和方法方面的专业知识。 法国研究人员在蛋白质折叠动力学研究方面的专业知识对此进行了补充。 该研究将促进我们对生物大分子结构与功能关系的理解。