| Autor: |
Ribeiro AA, Wemmer D, Bray RP, Wade-Jardetzky NG, Jardetzky O |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 1981 Feb 17; Vol. 20 (4), pp. 823-9. |
| DOI: |
10.1021/bi00507a026 |
| Abstrakt: |
The 360-MHz 1H NMR spectrum of native lac repressor headpiece (HP-51 or HP-59) contains a large number (greater than 30%) of aliphatic side-chain methyl and backbone alpha-CH resonances and three of four aromatic tyrosine multiplet resonances shifted to high-field chemical shift positions, indicating the presence of extensive folded structure. Denaturation leads to loss of the NMR chemical shift differences. Resonance identifications of the 27 methyl-possessing amino acids in HP-59 have been made by using resolution enhancement, double-resonance, and difference spectra. There are three firmly assigned methyl resonances and 21 pairwise identifications of methyl resonances in HP-51. Comparison of HP-51 and HP-59 allows identification of four additional methyl groups in amino acid residues 52--59. The sequence HP-50--59 is not essential to maintain the structure of HP-59, but it is of interest itself as the flexible hinge portion connecting HP to the tetrameric core of whole repressor. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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