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C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4.
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- Genes to Cells, 2016, v. 21, n. 3, p. 252, doi. 10.1111/gtc.12339
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Solution structure of the isolated histone H2A-H2B heterodimer.
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- Scientific Reports, 2016, p. 24999, doi. 10.1038/srep24999
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- Article
Important role of methionine 145 in dimerization of bovine β-lactoglobulin.
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- Journal of Biochemistry, 2012, v. 151, n. 3, p. 329, doi. 10.1093/jb/mvr142
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- Article
Structure and stability of Gyuba, a β-lactoglobulin chimera.
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- Protein Science: A Publication of the Protein Society, 2011, v. 20, n. 11, p. 1867, doi. 10.1002/pro.720
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- Article
Relationship between chain collapse and secondary structure formation in a partially folded protein.
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- Biopolymers, 2014, v. 101, n. 6, p. 651, doi. 10.1002/bip.22433
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- Article
FACT modulates the conformations of histone H2A and H2B N-terminal tails within nucleosomes.
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- Communications Biology, 2022, v. 5, n. 1, p. 1, doi. 10.1038/s42003-022-03785-z
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- Article