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- W2038084181 abstract "Deletion of the 13 C-terminal residues of the 149 residue staphylococcal nuclease (SNase) molecule results in a denatured, partially unfolded molecule (SNaseΔ) that is relatively compact under physiological conditions. We have performed molecular dynamics simulations of wild type SNase and SNaseΔ at 300 K in aqueous solution. Whereas the wild type preserved its native three-dimensional architecture, the truncated form significantly denatures over the 500 ps simulation period. The denaturation leads to significant rearrangements in the inhibitor binding pocket and is in general accord with conformation-dependent chemical cleavage experiments. SNaseΔ thus provides a system in which protein denaturation can be examined using molecular dynamics under experimental conditions and at physiological temperatures." @default.
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- W2038084181 date "1996-01-01" @default.
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- W2038084181 title "Denaturation of Truncated Staphylococcal Nuclease in Molecular Dynamics Simulation at 300 K" @default.
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- W2038084181 doi "https://doi.org/10.1021/ja960095y" @default.
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