De Meutter Joëlle, Goormaghtigh Erik
Center for Structural Biology and Bioinformatics, Laboratory for the Structure and Function of Biological Membranes, Campus Plaine CP206/02, Brussels, Belgium.
Université Libre de Bruxelles CP206/2, B1050 Brussels, Belgium.
Comput Struct Biotechnol J. 2020 Jul 10;18:1864-1876. doi: 10.1016/j.csbj.2020.07.001. eCollection 2020.
While several Raman, CD or FTIR spectral libraries are available for well-characterized proteins of known structure, proteins themselves are usually very difficult to acquire, preventing a convenient calibration of new instruments and new recording methods. The problem is particularly critical in the field of FTIR spectroscopy where numerous new methods are becoming available on the market. The present papers reports the construction of a protein library (cSP92) including commercially available products, that are well characterized experimentally for their purity and solubility in conditions compatible with the recording of FTIR spectra and whose high-resolution structure is available. Overall, 92 proteins were selected. These proteins cover well the CATH space at the level of classes and architectures. In terms of secondary structure content, an analysis of their high-resolution structure by DSSP shows that the mean content in the different secondary structures present in cSP92 is very similar to the mean content found in the PDB. The 92-protein set is analyzed in details for the distribution of helix length, number of strands in β- sheets, length of β-strands and amino acid content, all features that may be important for the interpretation of FTIR spectra.
虽然有几个拉曼光谱、圆二色光谱或傅里叶变换红外光谱库可用于已知结构且特征明确的蛋白质，但蛋白质本身通常很难获得，这使得新仪器和新记录方法的校准变得不方便。这个问题在傅里叶变换红外光谱领域尤为关键，因为市场上有许多新方法可供使用。本文报道了一个蛋白质库（cSP92）的构建，该库包括市售产品，这些产品在与傅里叶变换红外光谱记录兼容的条件下，其纯度和溶解性经过实验充分表征，并且具有高分辨率结构。总共选择了92种蛋白质。这些蛋白质在类别和结构水平上很好地覆盖了CATH空间。就二级结构含量而言，通过DSSP对其高分辨率结构进行分析表明，cSP92中存在的不同二级结构的平均含量与蛋白质数据库（PDB）中发现的平均含量非常相似。对这92种蛋白质组成的集合进行了详细分析，包括螺旋长度分布、β折叠中的链数、β链长度和氨基酸含量，所有这些特征对于傅里叶变换红外光谱的解释可能都很重要。
