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- W1973015989 abstract "The hierarchal levels of internal movements of proteins may determine their functional processes; however the functional role of torsion vibrations of protein backbone is still ambiguous. We study the characteristic features of protein backbone vibrations and their relations with the protein conformational states. We used molecular dynamics simulations to determine the backbone rotational angles of each amino acid with femtosecond resolution in different conformational states. The time series of the angles were Fourier transformed and filtered to produce the power spectra of the rotations. For each amino acid, characteristic rotational spectra consisting of specific peaks in the 5-60 THz (150-1800 cm-1) region were found beside the lower frequency normal torsional peaks of free amino acids. The positions of the spectral peaks were stable on the nanosecond timescale. Interestingly, amino acids of the proteins could be classified into 10 distinct groups based on the specific part (5-60 THz) of their spectra. Very similar classes can be found in different proteins. We observed that the spectra of certain functional amino acids were altered between different conformational states." @default.
- W1973015989 created "2016-06-24" @default.
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- W1973015989 date "2011-02-01" @default.
- W1973015989 modified "2023-10-16" @default.
- W1973015989 title "Rotational Power Spectra of Protein Backbone" @default.
- W1973015989 doi "https://doi.org/10.1016/j.bpj.2010.12.1443" @default.
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