Lucent Del, England Jeremy, Pande Vijay
Biophysics Program, Stanford University, Stanford, CA, USA.
Phys Biol. 2009 Feb 10;6(1):015003. doi: 10.1088/1478-3975/6/1/015003.
Despite their immense importance to cellular function, the precise mechanism by which chaperonins aid in the folding of other proteins remains unknown. Experimental evidence seems to imply that there is some diversity in how chaperonins interact with their substrates and this has led to a number of different models for chaperonin mechanism. Computational methods have the advantage of accessing temporal and spatial resolutions that are difficult for experimental techniques; therefore, these methods have been applied to this problem for some time. Here we review the relevant computational models for chaperonin function. We propose that these models need not be mutually exclusive and in fact can be thought of as a set of tools the chaperonin may use to aid in the folding of a diverse array of substrate proteins. We conclude with a discussion of the role of water in the chaperonin mechanism, a factor that until recently has been largely neglected by most computational studies of chaperonin function.
尽管伴侣蛋白对细胞功能极为重要，但其协助其他蛋白质折叠的精确机制仍不为人知。实验证据似乎表明，伴侣蛋白与底物相互作用的方式存在一定差异，这导致了多种不同的伴侣蛋白作用机制模型。计算方法具有获得实验技术难以达到的时间和空间分辨率的优势；因此，这些方法已应用于该问题一段时间了。在此，我们综述了有关伴侣蛋白功能的相关计算模型。我们认为这些模型并非相互排斥，实际上可以被视为伴侣蛋白可能用来协助多种底物蛋白折叠的一组工具。我们最后讨论了水在伴侣蛋白机制中的作用，这一因素在大多数关于伴侣蛋白功能的计算研究中直到最近都基本被忽视了。
