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- W2090209751 abstract "Abstract Physicochemical study of nonhistone protein HMG14 from calf thymus has been undertaken. The protein has a random structure with a molecular weight of approximately 10,000. On interaction with DNA, it behaves like histones and nonhistone protein HMG17. Both circular dichroism and melting absorption technics show that the protein has an ionic interaction with DNA without causing significant changes in DNA structure. In conrast to HMG1 and HMG2 which reduce linking number of circular DNA, nonhistone protein HMG14 and HMG17 do not introduce any changes in topological winding number of DNA." @default.
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- W2090209751 date "1978-12-01" @default.
- W2090209751 modified "2023-10-05" @default.
- W2090209751 title "Conformational study of calf thymus HMG14 nonhistone protein" @default.
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- W2090209751 doi "https://doi.org/10.1016/0006-291x(78)91157-9" @default.
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