NMR and structural data for Connexin 32 and Connexin 26 N-terminal peptides.
NMR and structural data for Connexin 32 and Connexin 26 N-terminal peptides.
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Connexin 32 和 Connexin 26 N 端肽的 NMR 和结构数据。
DOI：
10.1016/j.dib.2016.08.044
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发表时间：
2016
期刊：
影响因子：
1.2
通讯作者：
Dowd,TerryL
中科院分区：
文献类型：
--
作者：
Batir,Yuksel;Bargiello,ThaddeusA;Dowd,TerryL
在这篇文章中，我们提出了连接蛋白26 （Cx26）、Cx26G12R和Cx32G12R突变体的1H和13c化学位移分配、二级结构倾向数据和归一化温度系数数据，分别在综合征性耳聋和夏可氏乳牙病中发现，发表在“连接蛋白26和连接蛋白32 n端突变体的结构研究使用1H NMR波谱”（Y. Batir， T.A. Bargiello， T.L. Dowd, 2016）[1]。突变G12R对Cx26和Cx32肽结构的影响不同。我们提供了二级结构倾向化学位移分析的数据，该分析使用Cα和Cβ质子的13c二级化学位移之间的差异来计算无序或折叠肽和蛋白质的二级结构倾向（SSP）评分。该数据补充了NOESY数据[1]计算的核磁共振结构。我们提出并比较了Cx26与Cx26G12R肽以及Cx32和Cx32G12R肽的SSP数据。此外，我们还提供了先前收集的Cx26、Cx26G12R和Cx32G12R肽的温度系数图[1]，并将其归一化为随机线圈温度系数，“随机线圈1H化学位移作为温度和三氟乙醇浓度的函数获得肽系列GGXGG”（G. Merutka， H.J. Dyson， P.E. Wright, 1995）[2]。这些归一化温度系数的降低可以直接观察到肽的不同片段的残基，这些数据告诉我们NH质子和NH质子的溶剂可及性，由于氢键的形成，NH质子可能受到更多的限制。
In this article we present1H and13C chemical shift assignments, secondary structural propensity data and normalized temperature coefficient data for N-terminal peptides of Connexin 26 (Cx26), Cx26G12R and Cx32G12R mutants seen in syndromic deafness and Charcot Marie Tooth Disease respectively, published in “Structural Studies of N-Terminal Mutants of Connexin 26 and Connexin 32 Using 1H NMR Spectroscopy” (Y. Batir, T.A. Bargiello, T.L. Dowd, 2016) [1]. The mutation G12R affects the structure of both Cx26 and Cx32 peptides differently. We present data from secondary structure propensity chemical shift analysis which calculates a secondary structure propensity (SSP) score for both disordered or folded peptides and proteins using the difference between the13C secondary chemical shifts of the Cα and Cβ protons. This data supplements the calculated NMR structures from NOESY data [1]. We present and compare the SSP data for the Cx26 vs Cx26G12R peptides and the Cx32 and Cx32G12R peptides. In addition, we present plots of temperature coefficients obtained for Cx26, Cx26G12R and Cx32G12R peptides collected previously [1] and normalized to their random coil temperature coefficients, “Random coil 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG” (G. Merutka, H.J. Dyson, P.E. Wright, 1995) [2]. Reductions in these normalized temperature coefficients are directly observable for residues in different segments of the peptide and this data informs on solvent accessibility of the NH protons and NH protons which may be more constrained due to the formation of H bonds.