Condensation of polynucleosome by histone H1 binding |
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| Authors: | F Watanabe |
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| Institution: | 1. Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow, 117312 USSR;2. Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-10691 Stockholm, Sweden |
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| Abstract: | The complete amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria is reported. The protein contains 190 amino acids and has a molecular mass of 20 967. Its structure is characterized by a concentration of charged amino acids in the two terminal segments (N 1-77 and C 128-190) of the protein, whereas its central region is more hydrophobic. The earlier reported homology of the protein with the delta-subunit of E. coli F1, based on the terminal amino acid sequences of OSCP, is further substantiated. |
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| Keywords: | Amino acid sequence Oligomycin sensitivity-conferring protein Homology Amino acid residue SDS sodium dodecyl sulphate PTH phenylthiohydantoin OSCP oligomycin sensitivity-conferring protein |
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