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• W2035693704 startingPage "2341" @default.
• W2035693704 abstract "The crystallographic structure of bovine prothrombin fragment 1 bound with calcium ions was used to construct the corresponding human prothrombin structure (hf1/Ca). The model structure was refined by molecular dynamics to estimate the average solution structure. Accommodation of long-range ionic forces was essential to reach a stable solution structure. The gamma-carboxyglutamic acid (Gla) domain and the kringle domain of hf1/Ca independently equilibrated. Likewise, the hydrogen bond network and the calcium ion coordinations were well preserved. A discussion of the phospholipid binding of the vitamin K-dependent coagulation proteins in the context of the structure and mutational data of the Gla domain is presented." @default.
• W2035693704 created "2016-06-24" @default.
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• W2035693704 date "1995-11-01" @default.
• W2035693704 modified "2023-10-17" @default.
• W2035693704 title "Homology modeling and molecular dynamics simulation of human prothrombin fragment 1" @default.
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• W2035693704 doi "https://doi.org/10.1002/pro.5560041112" @default.
• W2035693704 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2143007" @default.
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