Rogers S W, Rechsteiner M
Department of Biology, University of Utah, Salt Lake City 84132.
J Biol Chem. 1988 Dec 25;263(36):19850-62.
We have compared sequence and structural features of 35 proteins to their metabolic stabilities in HeLa cells. No relationship was observed between the half-life of an injected protein and its subunit molecular weight, isoelectric point, hydrophobicity, thermostability, surface charge density, or N-terminal residue. Other properties, including susceptibility to oxidation, specific combinations of amino acids, secondary structure composition, and solvent exposed residues, also failed to correlate with protein stability. Although a weak inverse correlation was obtained when stability was compared to asparagine and glutamine content, we conclude that the degradation of an injected protein is unlikely to be related to any single structural parameter. Rather, we hypothesize that it results from an interplay between subcellular location and still poorly defined surface features of the injected proteins.
我们已将35种蛋白质的序列和结构特征与其在HeLa细胞中的代谢稳定性进行了比较。未观察到注射蛋白的半衰期与其亚基分子量、等电点、疏水性、热稳定性、表面电荷密度或N端残基之间存在关联。其他特性，包括氧化敏感性、特定氨基酸组合、二级结构组成以及溶剂暴露残基，也与蛋白质稳定性无关。尽管在将稳定性与天冬酰胺和谷氨酰胺含量进行比较时获得了微弱的负相关，但我们得出结论，注射蛋白的降解不太可能与任何单一结构参数相关。相反，我们推测这是由亚细胞定位与注射蛋白表面特征仍不明确之间的相互作用导致的。
