Roterman Irena, Stapor Katarzyna, Dułak Dawid, Konieczny Leszek
Department of Bioinformatics and Telemedicine, Jagiellonian University-Medical College, Medyczna 7, 30-688 Krakow, Poland.
Department of Applied Informatics, Faculty of Automatic, Electronics and Computer Science, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland.
Int J Mol Sci. 2025 Jul 1;26(13):6360. doi: 10.3390/ijms26136360.
The contribution of the environment to protein folding seems obvious. The aqueous environment directs protein folding towards generating a centric hydrophobic core with a polar shell. The cell membrane environment-in which numerous proteins are anchored-to stabilise the arrangement, expects the exposure of hydrophobic residues and the concentration of polar residues in the central part-a channel for the transport of numerous molecules. The influence of these environments seems evident due to the persistent residence of proteins in their surroundings providing an external force field for structure stabilisation. Structural forms are also obtained with the participation of supporting proteins-such as proteins from the heat shock protein group-which accompany the folding process and temporarily provide an appropriate external force field in which the protein, having obtained the correct structure for its activity, is released from interaction with the supporting protein. This paper discusses an example of the contribution of Hsp104 to casein folding and the effect of disaggregase preventing inappropriate aggregation. For this purpose, a model called the fuzzy oil drop (FOD-M) was used, which takes hydrophobic interactions into account in the assessment of protein structure status. Their distribution in the protein body highlights the contribution and influence of the external force field-originating from Hsp104 and the disaggregase in this case.
环境对蛋白质折叠的贡献似乎是显而易见的。水性环境引导蛋白质折叠形成具有极性外壳的中心疏水核心。细胞膜环境（众多蛋白质锚定于此以稳定排列）则要求疏水残基暴露在外，而极性残基集中在中心部分，形成众多分子运输的通道。由于蛋白质持续存在于其周围环境中，为结构稳定提供了外部力场，这些环境的影响似乎很明显。结构形式的获得还得益于辅助蛋白（如热休克蛋白家族的蛋白质）的参与，它们伴随折叠过程，暂时提供合适的外部力场，蛋白质在获得其活性的正确结构后，便从与辅助蛋白的相互作用中释放出来。本文讨论了Hsp104对酪蛋白折叠的贡献以及解聚酶防止不适当聚集的作用的一个例子。为此，使用了一种称为模糊油滴（FOD-M）的模型，该模型在评估蛋白质结构状态时考虑了疏水相互作用。它们在蛋白质体内的分布突出了在这种情况下源自Hsp104和解聚酶的外力场的贡献和影响。
