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• W2067047618 abstract "The room-temperature tryptophan (Trp) phosphorescence lifetime is sensitive to details of the local environment and has been shown to increase significantly in some proteins following H-D exchange. Careful analysis of the phosphorescence lifetime distribution of Trp 109 in Escherichia coli alkaline phosphatase (AP) in solution as a function of time during the H-D exchange shows that this process corresponds to a two-state reaction resulting from the deuteration of a single, specific hydrogen in the core of the protein. The absence of a pH dependence of the exchange rate suggests that the exchange is not an EX2 process, and therefore, a certain degree of unfolding is required for exchange to occur. This discovery opens up the use of phosphorescence-detected hydrogen exchange as a sensitive tool for monitoring the local susceptibility and activation energy for exchange in proteins having a phosphorescent Trp and, for example, for studying the effects of local mutations upon that susceptibility." @default.
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• W2067047618 date "2000-01-19" @default.
• W2067047618 modified "2023-10-16" @default.
• W2067047618 title "Hydrogen Exchange at the Core of <i>Escherichia coli</i> Alkaline Phosphatase Studied by Room-Temperature Tryptophan Phosphorescence" @default.
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• W2067047618 doi "https://doi.org/10.1021/bi991560h" @default.
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