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Low-frequency collective motion in proteins and DNA refers to the application of statistical thermodynamics to understand low-frequency vibrations in biomolecules. The concept of low-frequency phonons (or internal motion) in proteins was originally proposed by Professor Kuo-Chen Chou and Professor Nian-Yi Chen in order to solve a perplexing “free-energy deficit” problem in protein binding.〔 In studying the binding interaction between proteins such as insulin and insulin receptor, it was noted that enumerating the known explanations for the free energy change, such as translational and rotational entropy, hydrogen bonds, van der Waals interactions, and hydrophobic interactions, did not fully account for the observed free energy change for the reaction. It was inferred that the deficit could be explained by the creation of extra vibrational modes with very low wave numbers in the range of 10–100 cm−1, corresponding to the range of terahertz frequency (3×1011 to 3×1012 Hz).〔〔〔 Subsequently, the aforementioned low-frequency modes have been indeed observed by Raman spectroscopy for a number of protein molecules〔 and different types of DNA.〔〔 These observed results have also been further confirmed by neutron scattering experiments.〔〔Nickels JD, Perticaroli S, O’Neill H, Zhang Q, Ehlers G, Sokolov AP. Coherent Neutron Scattering and Collective Dynamics in the Protein, GFP. Biophysical journal 2013;105:2182-2187〕〔Perticaroli S, Nickels JD, Ehlers G, O'Neill H, Zhang Q, Sokolov AP. Secondary structure and rigidity in model proteins. Soft Matter 2013;9:9548-9556〕〔Perticaroli S, Nickels JD, Ehlers G, Sokolov AP. Rigidity, secondary structure, and the Universality of the Boson Peak in Proteins. Biophysical journal 2014;106:2667-2674〕 ==Experimental Results == The beta-barrel protein GFP has been shown by coherent neutron scattering to undergo collective motions of the secondary structural units at ~1 THz.〔 These motions are thought to be sensitive to local rigidity within proteins, revealing beta structures to be generically more rigid than alpha or disordered proteins.〔〔 抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Low-frequency collective motion in proteins and DNA」の詳細全文を読む スポンサード リンク
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