Abstract
To deepen our understanding of the principles determining the folding and functioning of globular proteins the determination of their three-dimensional structures must be supplemented with the characterization of their internal motions. Although dynamical events in proteins occur on time-scale ranging from femtoseconds to at least seconds, the physical properties of globular proteins are such that picosecond (ps) time-scale motions make a particularly important contribution to the internal fluctuations of the atoms from their mean positions.
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Dates
Type | When |
---|---|
Created | 16 years, 5 months ago (March 17, 2009, 11:50 a.m.) |
Deposited | 3 years, 10 months ago (Oct. 3, 2021, 5:18 a.m.) |
Indexed | 3 weeks, 4 days ago (Aug. 6, 2025, 9:45 a.m.) |
Issued | 34 years ago (Aug. 1, 1991) |
Published | 34 years ago (Aug. 1, 1991) |
Published Online | 16 years, 5 months ago (March 17, 2009) |
Published Print | 34 years ago (Aug. 1, 1991) |
@article{Smith_1991, title={Protein dynamics: comparison of simulations with inelastic neutron scattering experiments}, volume={24}, ISSN={1469-8994}, url={http://dx.doi.org/10.1017/s0033583500003723}, DOI={10.1017/s0033583500003723}, number={3}, journal={Quarterly Reviews of Biophysics}, publisher={Cambridge University Press (CUP)}, author={Smith, J. C.}, year={1991}, month=aug, pages={227–291} }