STUDIES ON CONFORMATIONAL PROPERTIES OF HIGH-MOBILITY-GROUP CHROMOSOMAL PROTEIN HMG 17 AND ITS INTERACTION WITH DNA
STUDIES ON CONFORMATIONAL PROPERTIES OF HIGH-MOBILITY-GROUP CHROMOSOMAL PROTEIN HMG 17 AND ITS INTERACTION WITH DNA
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DOI:
10.1111/j.1432-1033.1978.tb12154.x
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发表时间:
1978-01-01
期刊:
影响因子:
--
通讯作者:
JOHNS, EW
中科院分区:
文献类型:
--
作者:
ABERCROMBIE, BD;KNEALE, GG;JOHNS, EW
The conformation of the [calf thymus] non-histone chromatin protein, HMG 17, was studied using circular dichroism, IR and NMR spectroscopies, and by small-angle scattering. In free solution this protein has little or no secondary or tertiary structure, in contrast to the other high-mobility-group proteins, HMG 1 and 2, which exhibit highly ordered structures. Protein HMG 17 binds to calf thymus DNA in an ionic-dependent manner, precipitating the DNA at high protein/DNA ratio. The principle DNA-binding segment of HMG 17 is probably that between about residues 15-40.