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通过时间分辨傅里叶变换红外光谱监测蛋白质的分子反应机制。

Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy.

作者信息

Gerwert K

机构信息

Ruhr-Universität Bochum, Lehrstuhl für Biophysik, Germany.

出版信息

Biol Chem. 1999 Jul-Aug;380(7-8):931-5. doi: 10.1515/BC.1999.115.

Abstract

Time-resolved FTIR difference spectroscopy can provide a valuable insight into the molecular reaction mechanisms of proteins, especially membrane proteins. Isotopic labeling and site-directed mutagenesis allows an unequivocal assignment of IR absorption bands. Studies are presented which give insight into the proton pump mechanisms of proteins, especially bacteriorhodopsin. H-bonded network proton transfer via internal water molecules seems to be a general feature in proteins, also found in cytochrome c oxidase. Using caged GTP the intrinsic and GAP catalyzed GTPase activity of H-ras p21 is studied. Furthermore, protein folding reactions can be recorded with ns time-resolution.

摘要

时间分辨傅里叶变换红外差示光谱法能够为蛋白质尤其是膜蛋白的分子反应机制提供有价值的见解。同位素标记和定点诱变可实现红外吸收带的明确归属。本文展示了一些研究,这些研究深入探讨了蛋白质尤其是细菌视紫红质的质子泵机制。通过内部水分子进行的氢键网络质子转移似乎是蛋白质中的一个普遍特征,在细胞色素c氧化酶中也有发现。利用笼形鸟苷三磷酸研究了H-ras p21的内在和GAP催化的GTP酶活性。此外,蛋白质折叠反应可以以纳秒时间分辨率进行记录。

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