A consistent picture of protein dynamics. | Zendy

F. Parak | Zendy; ErnstWalter Knapp | Zendy

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A consistent picture of protein dynamics.

Author(s) -

F. Parak,

ErnstWalter Knapp

Publication year - 1984

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.81.22.7088

Subject(s) - myoglobin , protein dynamics , statistical physics , dynamics (music) , amplitude , molecular dynamics , flexibility (engineering) , entropy (arrow of time) , physics , transfer entropy , diffusion , chemistry , thermodynamics , principle of maximum entropy , computer science , mathematics , optics , quantum mechanics , artificial intelligence , statistics , organic chemistry , acoustics

Information about the protein dynamics of myoglobin obtained by x-ray and Mössbauer investigations is analyzed and compared with computer simulations. Computer simulations give correct amplitudes of mean-square displacements but fail in the description of the time dependence of motions. Our model describes protein dynamics at physiological temperatures as an overdamped diffusion-like motion in a restricted space. The fluctuations occur around the average conformation determined by x-ray structure analysis. The gain in entropy drives the molecule into the transition state and, in this way, accounts for its flexibility.

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