TIME-RESOLVED MAGNETIC CIRCULAR DICHROISM
时间分辨磁圆二色性
基本信息
- 批准号:2900657
- 负责人:
- 金额:$ 18.05万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1987
- 资助国家:美国
- 起止时间:1987-07-01 至 2000-03-31
- 项目状态:已结题
- 来源:
- 关键词:biomedical equipment development chemical kinetics circular magnetic dichroism conformation cytochrome b cytochrome c cytochrome oxidase electron transport enzyme mechanism enzyme structure hemoglobin hemoprotein structure magnetic field method development molecular dynamics mutant photochemistry photolysis protein structure function structural biology time resolved data ultraviolet radiation
项目摘要
DESCRIPTION: Development and use of time resolved magnetic circular
dichroism spectroscopy (TRMCD) is proposed. The application of a
magnetic field induces chirality and the observed signal is generally
localized to the moiety who's absorption is being probed. This
technique is used for heme centers. Extension of the technique to the
near UV is to be developed, and preliminary data on the static MCD of
tryptophan is encouraging (will require an extra electromagnet to
compensate for the Faraday rotation of the cell windows). The central
idea is to photolyze a ligand and then study the kinetics. The
resolution of the TRMCD apparatus is about 50-100 ns in the heme center
absorption (partly complicated by signals that result from the protein
diffusional reorientation time, about 100 ns- this complication has been
analyzed and is probably correctable). Studies on cytochrome oxidase,
cytochrome c3, and cytochrome c' are ongoing. A particularly important
finding of the past period was the finding of a transient ligation at the
cytochrome a3 site of cytochrome oxidase, resulting in a model for part
of the gating mechanism coupling energy release by oxygen reduction to
proton pumping (the ligand shuttle model). An unknown ligand in the
protein binds to the protein iron center and this has been best studied
with this technique. Most interesting future studies center on
hemoglobin and the R to T allosteric transition, if the trp residues can
be isolated and measured. Some hope has been demonstrated by static MCD
on trp in solution. Mutants should isolate which trp residues yield
signal. Recent TRCD results, just submitted to Biochemistry, are
exciting. Outstanding studies except there were two problems cited in
last review: the problem of protein orientational relaxation, which is
on the 100 ns time scale, and the issue of productivity.
描述:时间分辨磁环的开发和应用
提出了二向色性光谱(TRMCD)。的应用程序
磁场产生手性,观测到的信号一般是
定位到正在被探测的吸收的那一部分。这
这项技术被用于血红素中心。将这项技术推广到
近紫外线将被开发,关于静态MCD的初步数据
色氨酸是令人鼓舞的(将需要额外的电磁铁
补偿单元窗口的法拉第旋转)。中环
想法是光解一种配体,然后研究其动力学。这个
TRMCD装置在血红素中心的分辨率约为50-100 ns
吸收(由蛋白质产生的信号使吸收部分复杂化
弥散重定向时间,大约100 ns-这个并发症已经
分析并可能是可纠正的)。细胞色素氧化酶的研究,
细胞色素C3和细胞色素C‘正在进行中。一个特别重要的问题
过去一段时间的发现是在交界处发现了短暂的结扎
细胞色素A3位点的细胞色素氧化酶,导致部分模型
结合氧还原释放能量的浇注机制
质子泵浦(配体穿梭模型)。一种未知的配体
蛋白质结合到蛋白质铁中心,这一点已经得到了最好的研究
用这种技术。未来最有趣的研究集中在
血红蛋白和R到T的变构转变,如果Trp残基可以
被隔离和测量。静态MCD显示出了一些希望
关于溶液中的色氨酸。突变体应分离出哪些色氨酸残基产生
信号。最近的TRCD结果,刚刚提交给生物化学,是
令人兴奋。优秀的研究,除了在
最后一篇综述:蛋白质取向驰豫的问题,即
在100纳秒的时间尺度上,以及生产力的问题上。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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DAVID S. KLIGER其他文献
DAVID S. KLIGER的其他文献
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{{ truncateString('DAVID S. KLIGER', 18)}}的其他基金
Fast Kinetic Studies of Protein Folding and Function
蛋白质折叠和功能的快速动力学研究
- 批准号:
7098013 - 财政年份:2004
- 资助金额:
$ 18.05万 - 项目类别:
Fast Kinetic Studies of Protein Folding and Function
蛋白质折叠和功能的快速动力学研究
- 批准号:
6874802 - 财政年份:2004
- 资助金额:
$ 18.05万 - 项目类别:
Fast Kinetic Studies of Protein Folding and Function
蛋白质折叠和功能的快速动力学研究
- 批准号:
6945191 - 财政年份:2004
- 资助金额:
$ 18.05万 - 项目类别:
Fast Kinetic Studies of Protein Folding and Function
蛋白质折叠和功能的快速动力学研究
- 批准号:
7270641 - 财政年份:2004
- 资助金额:
$ 18.05万 - 项目类别:
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