1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein.
1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein.
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HMG-I 蛋白小沟 DNA 结合肽的 1H 和 13C NMR 归属和分子建模。
DOI:
10.1111/j.1399-3011.1995.tb01319.x
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发表时间:
1995
期刊:
影响因子:
--
通讯作者:
Reeves,R
中科院分区:
文献类型:
--
作者:
Evans,JN;Zajicek,J;Nissen,MS;Munske,G;Smith,V;Reeves,R
The HMG‐I subfamily of high mobility group (HMG) chromatin proteins consists of DNA‐binding proteins that preferentially bind to stretches of A·T‐rich sequence bothin vitroandin vivo.Recently, members of the HMG‐I family have been suggested to bindin vitroto the narrow minor groove of A·T‐DNA by means of an 11 amino acid peptide binding domain (BD) which, because of its predicted structure, is called the‘A·T‐hook motif [Reeves, R. & Nissen, M. (1990)J. Biol. Chem.265, 8573–8582], and would appear to be crescent‐shaped. A BD peptide with 13 amino‐acid residues was synthesized and examined by proton and carbon‐13 nuclear magnetic resonance (NMR) spectroscopy. The peptide contains four proline residues, and on the basis of NOES and13C chemical shifts was found to exist in an all‐transconformation. Molecular modelling based on this result provides evidence for a dynamic equilibrium between turn‐like conformations in solution, the most populated of which is likely to be an S‐shaped conformer, on the basis of amide exchange data. © Munksgaard 1995.