2016
DOI: 10.1016/j.jbiosc.2016.01.005
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Cooperative hydration effect causes thermal unfolding of proteins and water activity plays a key role in protein stability in solutions

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Cited by 11 publications
(1 citation statement)
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“…Another noticeable difference are the values obtained for ∆Hm, which is almost reduced to half in the T10C-(CH2)3O(CH2)2O(CH2)3-T10C polymer (58.2 ± 0.6 kcal/mol vs 101.4 ± 0.4 kcal/mol obtained for DpsT10C). A possible interpretation for this difference is the expected collaborative effect on the disruption of hydrogen bonding, and other non-covalent molecular interactions 37 , in addition to a more favorable hydration of the denatured state for the polymeric T10C-(CH2)3O(CH2)2O(CH2)3-T10C protein.…”
Section: Resultsmentioning
confidence: 99%
“…Another noticeable difference are the values obtained for ∆Hm, which is almost reduced to half in the T10C-(CH2)3O(CH2)2O(CH2)3-T10C polymer (58.2 ± 0.6 kcal/mol vs 101.4 ± 0.4 kcal/mol obtained for DpsT10C). A possible interpretation for this difference is the expected collaborative effect on the disruption of hydrogen bonding, and other non-covalent molecular interactions 37 , in addition to a more favorable hydration of the denatured state for the polymeric T10C-(CH2)3O(CH2)2O(CH2)3-T10C protein.…”
Section: Resultsmentioning
confidence: 99%