High resolution proton magnetic resonance spectroscopy of histones and histone--histone complexes in aqueous solution
| Autor: | Fulmer Aw, Gerald D. Fasman, Nicos A. Nicola, Schwartz Am |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Erythrocytes
Magnetic Resonance Spectroscopy Arginine Chemical Phenomena Macromolecular Substances Dimer Lysine Analytical chemistry Biochemistry Histones chemistry.chemical_compound Tetramer Animals chemistry.chemical_classification Alanine Aqueous solution biology Amino acid Molecular Weight Crystallography Chemistry Histone chemistry biology.protein Protons Chickens |
| Zdroj: | Biochemistry. 17(9) |
| ISSN: | 0006-2960 |
| Popis: | Low molecular weight histone complexes of H2A (congruent to dimer), H2B (congruent to tetramer), H3--H4 (congruent to tetramer), H2A--H2B (congruent to dimer), and H2B--H4 (congruent to dimer) have been prepared in 2 M NaCl and neutral pH at 4 degrees C. These materials are free of nonspecific aggregate and are suitable for study by high resolution proton magnetic resonance spectroscopy. Such spectra have been recorded in aqueous solutions under conditions allowing a study of the exchangeable proton resonances of histone complexes for the first time and indicate that the structured regions are rich in hydrophobic amino acids, as well as arginine and some acidic amino acids. Most of the lysine and probably alanine residues remain in a motile, random coil-like state after formation of the complexes. It is suggested that arginine residues may be important in inter- and/or intra-subunit interactions in histone complexes. |
| Databáze: | OpenAIRE |
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