U.S.-Brazil Cooperative Research on The Medium Dependence ofBiological Electron Transfer Reactions

该奖项支持由加州理工学院的John J. Hopfield教授、喷气推进实验室（Caltech）的David Beratan博士和圣保罗大学圣卡洛斯物理与化学研究所的Jose Nelson Onuchic教授在分子生物物理学方面进行的合作研究。巴西。他们将构建蛋白质中生物电荷（电子）转移反应的微观预测模型。具体地说，预测血红素蛋白异构体中电子转移的相对速率（以及距离和温度依赖）将被开发。这些电子转移反应是生物系统中几乎所有能量过程的基础，因此是目前非常感兴趣的。Hopfield教授和Beratan博士都将访问圣卡洛斯。只有Beratan博士的旅费将由这笔拨款支付。他们将与Onuchic教授合作，计算肌红蛋白衍生物中不同异构体的基质元素，此前在巴西和美国以不同的方式检测了肌红蛋白的晶体结构。将计算输运温度的依赖关系，并考虑新的计算方法。最后计算出电子传递的分子参数。喷气推进实验室的先进计算设备（Cray）将与巴西的VAX以及巴西研究蛋白质动力学的试验组使用的EPR和光学技术一起使用。重要的科学贡献将由这些小组单独完成。

This award supports cooperative research in molecular biophysics to be conducted by Prof. John J. Hopfield at the California Institute of Technology and Dr. David Beratan of the Jet Propulsion Laboratory (Caltech) and Prof. Jose Nelson Onuchic of the Sao Carlos Institute of Physics and Chemistry, University of Sao Paulo, Brazil. They will construct a microscopic predictive model for biological charge (electron) transfer reactions in proteins. Specifically, predictions for the relative rates (and distance and temperature dependence) of electron transfer in isomers of heme proteins will be developed. These electron tranfer reactions are basic to nearly all energetic processes in biological systems and therefore are of great interest at the present time. Both Prof. Hopfield and Dr. Beratan will visit San Carlos. Only Dr. Beratan's travel will be supported by this grant. They will work with Prof. Onuchic to calculate matrix elements for different isomers in myoglobin derivatives after myoglobin crystal structures have been examined in different ways in both Brazil and the U.S. During visits to Caltech by Prof. Onuchic, transport temperature dependence will be calculated and new methods of calculation will be considered. Finally the molecular parameters of electron transfer will be worked out. The advanced computing facilities (Cray) at JPL will be used along with a VAX in Brazil as well as EPR and optical techniques in use by Brazilian experimental groups studying protein dynamics. Important scientific contributions will be made that could not be done so well by these groups working alone.