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• W3204289807 abstract "The interface between hemoglobin (Hb) and its environment, in particular water, is of great physiological relevance. Here, results from {it in vitro}, {it in vivo}, and computational experiments (molecular dynamics simulations) are summarized and put into perspective. One of the main findings from the computations is that the stability of the deoxy, ligand-free T-state (T$_0$) can be stabilized relative to the deoxy R-state (R$_0$) only in sufficiently large simulation boxes for the hydrophobic effect to manifest itself. This effect directly influences protein stability and is operative also under physiological conditions. Furthermore, molecular simulations provide a dynamical interpretation of the Perutz model for Hb function. Results from experiments using higher protein concentrations and realistic cellular environments are also discussed. One of the next great challenges for computational studies, which as we show is likely to be taken up in the near future, is to provide molecular-level understanding of the dynamics of proteins in such crowded environments." @default.
• W3204289807 created "2021-10-11" @default.
• W3204289807 creator A5010154021 @default.
• W3204289807 creator A5076499540 @default.
• W3204289807 date "2021-10-07" @default.
• W3204289807 modified "2023-09-23" @default.
• W3204289807 title "The Functional Role of the Hemoglobin-Water Interface" @default.
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• W3204289807 hasPublicationYear "2021" @default.
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