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首页> 外文期刊>Journal of magnetic resonance >Protein Dynamics Measurements by TROSY-Based NMR Experiments
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Protein Dynamics Measurements by TROSY-Based NMR Experiments

机译：通过基于TROSY的NMR实验测量蛋白质动力学

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摘要

The described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T_1, T_2, and NOE of backbone ~(15)N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-PT sequence from the HSQC-based experiments. This has the benefit of shortening the pulse sequences by 5.4 ms (=1/2J) and results in an increase in the intrinsic sensitivity of the proposed TROSY-based experiments. The TROSY-based experiments are on average of 13% more sensitive than the corresponding HSQC-based experiments on a uniformly ~(15)N-labeled Xenopus laevis calcium-bound calmodulin sample on a 750-MHz spectrometer at 5℃. The amide proton linewidths of the TROSY-based experiments are 2-13 Hz narrower than those of the HSQC experiments. More sensitivity gain and higher resolution are expected if the protein sample is deuterated.
机译：所描述的基于TROSY的用于研究蛋白质骨架动态的实验使得通过测量骨架〜（15）N核的T_1，T_2和NOE阐明大型蛋白质的内部运动成为可能。在我们提出的序列中，从基于HSQC的实验中消除了INEPT序列，并用ST2-PT序列取代了PEP序列。这具有将脉冲序列缩短5.4 ms（= 1 / 2J）的好处，并提高了所提出的基于TROSY的实验的固有灵敏度。在5°C的750 MHz光谱仪上，均匀地〜（15）N标记的非洲爪蟾钙结合钙调蛋白样品的基于TROSY的实验平均比相应的基于HSQC的实验敏感13％。基于TROSY的实验的酰胺质子线宽比HSQC实验的窄2-13 Hz。如果将蛋白质样品氘化，则有望获得更高的灵敏度和更高的分辨率。

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