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• W2072949618 abstract "The dynamic nature of protein function is a fundamental concept in the physics of proteins. Although the basic general ideas are well accepted most experimental evidence has an indirect nature. The detailed characterization of the dynamics is necessary for the understanding in detail. The dynamic fluctuations thought crucial for the function span an extremely broad time, starting from the picosecond regime. Recently, a few new experimental techniques emerged that permit the observation of dynamical phenomena directly. Notably, pulsed infrared (IR) spectroscopy has been applied with great success to observe structural changes with picosecond time resolution. Using two‐dimensional‐IR vibrational echo chemical exchange spectroscopy Ishikawa and co‐workers [Ishikawa et al. (2008), Proc. Natl. Acad. Sci. U.S.A. 101, 14402–14407] managed to observe the transition between well defined conformational substrates of carbonmonoxy myoglobin directly. This is an important step in improving our insight into the details of protein function." @default.
• W2072949618 created "2016-06-24" @default.
• W2072949618 creator A5080135690 @default.
• W2072949618 date "2008-12-01" @default.
• W2072949618 modified "2023-10-16" @default.
• W2072949618 title "Dynamic fluctuation of proteins watched in real time" @default.
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• W2072949618 doi "https://doi.org/10.2976/1.2978985" @default.
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