Scaling of Rates of Vibrational Energy Transfer in Proteins with Equilibrium Dynamics and Entropy
| Autor: | David M. Leitner, Korey M. Reid, Takahisa Yamato |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein Conformation Entropy Inverse Molecular Dynamics Simulation 010402 general chemistry Vibration 01 natural sciences Power law 03 medical and health sciences Molecular dynamics Materials Chemistry Physical and Theoretical Chemistry Entropy (energy dispersal) Scaling Physics Myoglobin Hydrogen bond Hydrogen Bonding Conformational entropy 0104 chemical sciences Surfaces Coatings and Films 030104 developmental biology Energy Transfer Chemical physics Apoproteins |
| Zdroj: | The Journal of Physical Chemistry B. 122:9331-9339 |
| ISSN: | 1520-5207 1520-6106 |
| Popis: | Theoretical arguments and results of molecular dynamics (MD) simulations of myoglobin at 300 K are presented to relate rates of vibrational energy transfer across nonbonded contacts interacting via short-range potentials to dynamics of the contact. Both theory and the results of the simulations support a scaling relation between the energy transfer rate and the inverse of the variance in the distance between hydrogen-bonded contacts. The results of the MD simulations do not support such a relation for longer-range charged contacts. Instead, the energy transfer rate is found to scale as a power law in the distance between charged groups. The scaling between rates of vibrational energy transfer across nonbonded contacts interacting via short-range potentials and conformational dynamics suggests a relation between vibrational energy transfer rates and entropy associated with the dynamics of interacting residues. The use of time-resolved vibrational spectroscopy to determine change in conformational entropy with change in protein functional state is discussed, and an expression quantifying the connection is provided. |
| Databáze: | OpenAIRE |
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