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首页> 外文期刊>Biochemistry >Main chain and side chain dynamics of peptides in liquid solution from 13C NMR: melittin as a model peptide.
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Main chain and side chain dynamics of peptides in liquid solution from 13C NMR: melittin as a model peptide.

机译：肽在13C NMR液体溶液中的主链和侧链动力学：以蜂毒肽为模型肽。

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摘要

Peptide backbone and lysine and tryptophan side chain mobilities in the synthetic, 26-residue peptide melittin (MLT) enriched with 13C were investigated in liquid solution by 13C T1 and steady state nuclear Overhauser effect measurements at 2 magnetic fields and by Trp fluorescence anisotropy measurements and were analysed using the Lipari and Szabo model-free approach. The overall rotational correlation times at 20deg C were 1.28, 1.4, 2.8 and 4.2 ns for monomeric random coil MLT, for monomeric helical MLT (in CD3OD), for tetrameric MLT in neat D2O, and for the tetramer in 50 mM phosphate buffer, respectively. Motion of the backbone in the interior of the sequence was most restricted in the monomeric helix and least restricted in the tetramer. In the monomeric disordered peptide, relatively less restricted backbone motion extending from the N terminus to the 4th residue was observed. Such "end effects" continued only to the 3rd residue in the monomeric helix and were observed just in the amino terminus glycine in the tetramer. The 3 Lys side chains showed the least restricted motion in the monomers and a differential restriction in the tetramers consistent with the tetramer structure. The motion of the Trp side chain was more restricted than thatof Lys side chains and generally as restricted as that of the interior backbone atoms. The effective correlation times for the local motion of the backbone atoms were in the motional narrowing limit and showed distinct patterns. Agreement between NMR relaxation and Trp fluorescence anisotropy data was good for the monomer, but not for the tetramer. Implications of these results for peptide dynamics in general are examined.
机译：在13 C T1和2个磁场下的稳态核Overhauser效应测量以及在Trp荧光各向异性测量下，在液相溶液中研究了富含13C的合成的富含13C的26残基肽蜂毒素（MLT）中的肽骨架，赖氨酸和色氨酸侧链迁移率。使用Lipari和Szabo无模型方法进行了分析。对于单体无规卷曲MLT，对于单体螺旋MLT（在CD3OD中），对于纯D2O中的四聚体MLT和对于在50 mM磷酸盐缓冲液中的四聚体，在20℃下的总旋转相关时间分别为1.28、1.4、2.8和4.2 ns。 。骨架内部骨架的运动在单体螺旋中受到最大限制，而在四聚体中受到最小限制。在单体无序肽中，观察到从N末端延伸至第4个残基的限制性骨架运动相对较少。这种“末端效应”仅持续到单体螺旋中的第三个残基，并且仅在四聚体的氨基末端甘氨酸中观察到。 3个Lys侧链在单体中显示出最少的运动限制，并且在与四聚体结构一致的四聚体中显示出不同的限制性。 Trp侧链的运动比Lys侧链的运动更受限制，并且通常与内部骨架原子的运动一样受限制。骨架原子局部运动的有效相关时间在运动范围内，并表现出明显的规律。 NMR弛豫和Trp荧光各向异性数据之间的一致性对于单体是好的，但对于四聚体则不好。通常检查这些结果对肽动力学的影响。

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