Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure.
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چکیده
منابع مشابه
NUCLEAR MAGNETIC RESONANCE STUDY OF THE STRUCTURE OF GLYOXALDIHYDRAZONE
Study of the nuclear magnetic resonance spectra of glyoxaldihydrazone in dimethylsulfoxide and deuterochlorofonn leads to the conclusion that this compound exists predominantly in non-chelate structure
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study of the nuclear magnetic resonance spectra of glyoxaldihydrazone in dimethylsulfoxide and deuterochlorofonn leads to the conclusion that this compound exists predominantly in non-chelate structure
متن کاملThe polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics.
The polypeptide fold of the 79-residue globular domain of chicken histone H5 (GH5) in solution has been determined by the combined use of distance geometry and restrained molecular dynamics calculations. The structure determination is based on 307 approximate interproton distance restraints derived from n.m.r. measurements. The structure is composed of a core made up of residues 3-18, 23-34, 37...
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The globular domain of chicken histone H1 (GH1) has been studied by 1H homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy. After the full assignment of the proton and 15N resonances, the tertiary structure of GH1 was determined by an iterative procedure using distance geometry and restrained simulated annealing. The secondary structure elements of GH1, three helices (S5-A16, S24-A34, N42-...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1986
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.83.20.7628