Sodano P, Ptak M
Centre de Biophysique Moléculaire (CNRS), Orléans, France.
J Biomol Struct Dyn. 1995 Apr;12(5):1009-22. doi: 10.1080/07391102.1995.10508793.
COSY, TOCSY and NOESY experiments have been used to assign sequentially the 1H 500 MHz NMR spectra of the Hydrophobic Protein of Soybean (HPS). Spin systems identification combined with sequential assignment allowed to identify the proton resonances of this 80 residues protein. Analysis of medium range connectivities showed that its secondary structure involved four helical fragments similarly located as in the structure deduced from X-ray diffraction. This work set the basis for a further fine comparison between the crystal and the solution structures and a dynamical study of HPS in solution. In addition, search of secondary structure similarities showed that the global folding of HPS should be rather similar to that found for non specific Lipid Transfer Proteins (ns-LTP) from vegetal origin. Distributions of the helical fragments along the primary sequences of these two classes of proteins were compared.
已使用COSY、TOCSY和NOESY实验对大豆疏水蛋白（HPS）的1H 500 MHz NMR谱进行顺序归属。自旋系统鉴定与顺序归属相结合，得以鉴定出该80个残基蛋白质的质子共振峰。对中程连接性的分析表明，其二级结构包含四个螺旋片段，其位置与X射线衍射推导的结构相似。这项工作为进一步精细比较晶体结构和溶液结构以及对溶液中HPS进行动力学研究奠定了基础。此外，对二级结构相似性的搜索表明，HPS的整体折叠应该与植物来源的非特异性脂质转移蛋白（ns-LTP）相当相似。比较了这两类蛋白质一级序列上螺旋片段的分布。
