718 research outputs found
Multiplexed-Replica Exchange Molecular Dynamics with the UNRES Force-Field as an Effective Method for Exploring the Conformational Energy Landscape of Proteins.
Local structure involving histidine-12 in reduced S-sulfonated ribonuclease A detected by proton NMR spectroscopy under folding conditions.
Molecular dynamics simulations of the temperature-induced unfolding of crambin follow the Arrhenius equation
Molecular dynamics simulations have been used extensively to model the folding and unfolding of proteins. The rates of folding and unfolding should follow the Arrhenius equation over a limited range of temperatures. This study shows that molecular dynamic simulations of the unfolding of crambin between 500K and 560K do follow the Arrhenius equation. They also show that while there is a large amount of variation between the simulations the average values for the rate show a very high degree of correlation
Cold Inactivation of l-Threonine Deaminase from Rhodospirillum rubrum
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/66171/1/j.1432-1033.1971.tb01491.x.pd
The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding
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