Conformational features of peptide fragments of the C-end of histone H1
β Scribed by R. R. Kamilova; E. I. Ramm; G. S. Ivanov; L. I. Mar'yash; V. K. Burichenko
- Book ID
- 104851100
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 340 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0009-3130
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The synthetic peptide of sequence H-Ala-Ser-Thr-Thr-Thr-Am-Tyr-Thr-OH, termed peptide T, a competitor of the Human Immunodeficiency Virus in the binding to human T cells, and its C -t d a l pentapeptide fragment, were studied by 'H-nmr in DMSO solution to determine conformational preferences. The ob
Nucleosomal subunits isolated from rabbit thymus nuclei in 0.04 M K2SO 4-0.02 M Tris, pH 7.4 were devoid of histone H1, while whole chromatin prepared in the same buffer contained the full complement of histone HI. The question is asked why histone H1 dissociates from the subunits but not from the h