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• W2912665757 abstract "The effect of single amino acid mutations on the rebinding dynamics of nitrogen monoxide (NO) to myoglobin is investigated using reactive molecular dynamics simulations. In particular, mutations of residues surrounding the heme-active site (Leu29, His64, Val68) were considered. Consistent with experiments, all mutations studied here have a significant effect on the kinetics of the NO-rebinding process, which consists of a rapid (several 10 ps) and a slow (100s of ps) time scale. For all modifications considered, the time scales and rebinding fractions agree to within a few percents with results from experiments by adjusting one single, physically meaningful, conformationally averaged quantity: the asymptotic energy separation between the NO-bound (2A) and photodissociated (4A) states. It is furthermore shown that the thermodynamic stability of wild-type versus mutant Mb for the ligand-free and ligand-bound variants of the protein can be described by the same computational model. Therefore, ligand kinetics and thermodynamics are related in a direct fashion akin to Φ-value analysis, which establishes a relationship between protein folding rates and thermal stability of proteins." @default.
• W2912665757 created "2019-02-21" @default.
• W2912665757 creator A5010154021 @default.
• W2912665757 creator A5046506356 @default.
• W2912665757 creator A5066175948 @default.
• W2912665757 date "2019-02-06" @default.
• W2912665757 modified "2023-09-24" @default.
• W2912665757 title "Effect of Single-Point Mutations on Nitric Oxide Rebinding and the Thermodynamic Stability of Myoglobin" @default.
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• W2912665757 doi "https://doi.org/10.1021/acs.jpcb.8b11454" @default.
• W2912665757 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30724565" @default.
• W2912665757 hasPublicationYear "2019" @default.
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