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Measurement of protein associations via static light scattering

Measurement of protein associations via static light scattering
通过静态光散射测量蛋白质关联
批准号:
7593447
负责人:
Allen P Minton
金额:
$16.84万
依托单位国家:
美国
项目类别:
财政年份:
--
资助国家:
美国
项目状态:
未结题
起止时间:
至

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中文摘要
翻译
我们一直在测试由Wyatt Technology Incorporated设计的系统的预生产版本,以促进成分梯度静态光散射测量。 该系统基于我们实验室以前开发的概念,(参见前两年的年度报告),由一个泵模块和一个软件包组成,泵模块包含三个注射泵和一个在线脱气器,软件包用于控制注射器以创建成分梯度,从光散射和浓度检测器收集数据,并在单个蛋白质的平衡自缔合和两个蛋白质的异质缔合的模型的背景下分析数据。 硬件和软件由Wyatt Technology根据CRADA DK-05-0104条款借给我们。 初步结果表明,利用该系统,可以在单个实验中表征和量化两种单独蛋白质种类中的每一种的平衡自缔合和两种蛋白质的异质缔合,所述单个实验仅需要约2-3 mg的每种蛋白质和少于一小时的数据采集时间。
英文摘要
We have been testing pre-production versions of a system designed by Wyatt Technology Incorporated to facilitate composition-gradient static light scattering measurements. The system, based upon a concept developed previously in our laboratory (see annual reports of the previous two years), consists of a pump module containing three syringe pumps and an inline degasser, and a software package that is used to control the syringes to create composition gradients, to collect data from light scattering and concentration detectors, and to analyze the data in the context of models for equilibrium self-association of a single protein and hetero-association of two proteins. The hardware and software were loaned to us by Wyatt Technology under terms of CRADA DK-05-0104. Preliminary results indicate that with this system one can characterize and quantify equilibrium self-associations of each of two individual protein species and hetero-associations of the two proteins in a single experiment requiring only about 2-3 mg of each protein and less than one hour of data acquisition time.
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Noncovalent Intermolecular Interactions In Biochemistry
NONCOVALENT INTERMOLECULAR INTERACTIONS IN BIOCHEMISTRY
Thermodynamic and kinetic studies of macromolec structure and enzymic mechanisms
Studies of macromolecular crowding
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