19F NMR relaxation studies of fluorosubstituted tryptophans
19F NMR relaxation studies of fluorosubstituted tryptophans
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DOI：
10.1007/s10858-019-00268-y
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发表时间：
2019-09-01
影响因子：
2.7
通讯作者：
Gronenborn, Angela M.
中科院分区：
文献类型：
--
作者：
Lu, Manman;Ishima, Rieko;Gronenborn, Angela M.
我们目前的F-19纵向和横向弛豫研究四个不同的氟取代的L-色氨酸，其中携带单个F原子的吲哚环中，无论是在游离氨基酸的上下文中，当位于亲环蛋白A蛋白。对于游离的4F-、5 F-、6 F-、7 F-L-Trp，在实验测量的和计算的弛豫速率之间获得了令人满意的一致性，这表明用于计算吲哚框架的速率的参数是足够准确的。我们还测量和计算了四种不同的F-19-色氨酸标记亲环素A蛋白的弛豫速率，将参数从游离氨基酸转移到蛋白质结合部分。我们的研究结果表明，F-19弛豫数据的大型和刚性吲哚环色氨酸蛋白质运动的影响不大，并提供关键的参考点，为评估氟NMR弛豫在未来，特别是在氟色氨酸标记的蛋白质。
We present F-19 longitudinal and transverse relaxation studies for four differently fluorosubstituted L-tryptophans, which carry single F atoms in the indole ring, both in the context of the free amino acid and when located in the cyclophilin A protein. For the free 4F-, 5F-, 6F-, 7F-L-Trp, satisfactory agreement between experimentally measured and calculated relaxation rates was obtained, suggesting that the parameters used for calculating the rates for the indole frame are sufficiently accurate. We also measured and calculated relaxation rates for four differently F-19-tryptophan labeled cyclophilin A proteins, transferring the parameters from the free amino acid to the protein-bound moiety. Our results suggest that F-19 relaxation data of the large and rigid indole ring in Trp are only moderately affected by protein motions and provide critical reference points for evaluating fluorine NMR relaxation in the future, especially in fluorotryptophan labeled proteins.