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机构地区:[1]Shanghai Institute of Cell Biology, Academia Sinica, Shanghai 200031, PRC [2]Shanghai Institute of Nuclear Research, Academia Sinica, Shanghai 201800, PRC
出 处:《Science China Chemistry》1993年第8期933-939,共7页中国科学(化学英文版)
基 金:This work was supported by grants from Academia Sinica.
摘 要:The pattern of high mobility group proteins 1 and 2 (HMG1,2) interaction with the 5’-flanking sequence of the human β-globin gene has been analyzed by scanning tunnelling microscopy (STM). A 200 bp negative regulatory region in the 5’-flanking sequence of the human β-globin gene can be folded by HMG proteins 1 and 2 into a circular structure (diameter 70±6) with a linear tail which seems to be a left-handed double helix structure.The pattern of high mobility group proteins 1 and 2 (HMG1,2) interaction with the 5'-flanking sequence of the human β-globin gene has been analyzed by scanning tunnelling microscopy (STM). A 200 bp negative regulatory region in the 5'-flanking sequence of the human β-globin gene can be folded by HMG proteins 1 and 2 into a circular structure (diameter 70±6) with a linear tail which seems to be a left-handed double helix structure.
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