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首页> 外文期刊>Journal of Molecular Biology >NMR characterization of residual structure in the denatured state of protein L.
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NMR characterization of residual structure in the denatured state of protein L.

机译：蛋白质L变性状态下残留结构的NMR表征。

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摘要

Triple-resonance NMR experiments were used to assign the (13)C(alpha), (13)C(beta), (15)N and NH resonances for all the residues in the denatured state of a destabilized protein L variant in 2 M guanidine. The chemical shifts of most resonances were very close to their random coil values. Significant deviations were observed for G22, L38 and K39; increasing the denaturant concentration shifted the chemical shifts of these residues towards theory random coil values. Medium-range nuclear Overhauser enhancements were detected in segments corresponding to the turn between the first two strands, the end of the second strand through the turn between the second strand and the helix, and the turn between the helix and the third strand in 3D H(1), N(15)-HSQC-NOESY-HSQC experiments on perdeuterated samples. Longer-range interactions were probed by measuring the paramagnetic relaxation enhancement produced by nitroxide spin labels introduced via cysteine residues at five sites around the molecule. Damped oscillations in the magnitude of the paramagnetic relaxation enhancement as a function of distance along the sequence suggested native-like chain reversals in the same three turn regions. The more extensive interactions within the region corresponding to the first beta-turn than in the region corresponding to the second beta-turn suggests that the asymmetry in the folding reaction evident in previous studies of the protein L folding transition state is already established in the denatured state. Copyright 2000 Academic Press.
机译：使用三次共振NMR实验为2 M中不稳定L蛋白变体的变性状态下的所有残基指定（13）Cα，（13）Cβ，（15）N和NH共振胍。大多数共振的化学位移非常接近其随机线圈值。观察到G22，L38和K39的显着差异;增加变性剂浓度会使这些残基的化学位移向理论随机线圈值移动。在3D H中，在与前两个​​链之间的转弯，第二链的末端到第二链和螺旋之间的转弯以及螺旋和第三链之间的转弯相对应的片段中检测到了中程核Overhauser增强（1），对经氘化的样品进行的N（15）-HSQC-NOESY-HSQC实验。通过测量在分子周围五个位点通过半胱氨酸残基引入的一氧化氮自旋标记物产生的顺磁弛豫增强来探测更长距离的相互作用。顺磁性弛豫增强的幅度的阻尼振荡随沿着该距离的距离而变化，这表明在相同的三个转弯区域中存在类似天然链的逆转。在对应于第一β-转角的区域内比在对应于第二β-转角的区域内更广泛的相互作用表明，在变性的蛋白质L折叠过渡态的先前研究中明显的折叠反应中的不对称性已经建立。州。版权所有2000学术出版社。

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