Cruzeiro Leonor, Gill Andrew C, Eilbeck J Chris
CCMAR/CIMAR - Centro de Ciências do Mar, FCT, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal.
School of Chemistry, Joseph Banks Laboratories, University of Lincoln, Green Lane, Lincoln LN67DL, UK.
Biomolecules. 2021 Feb 26;11(3):357. doi: 10.3390/biom11030357.
We investigate the hypothesis that protein folding is a kinetic, non-equilibrium process, in which the structure of the nascent chain is crucial. We compare actual amino acid frequencies in loops, α-helices and β-sheets with the frequencies that would arise in the absence of any amino acid bias for those secondary structures. The novel analysis suggests that while specific amino acids exist to drive the formation of loops and sheets, none stand out as drivers for α-helices. This favours the idea that the α-helix is the initial structure of most proteins before the folding process begins.
蛋白质折叠是一个动力学的、非平衡过程，在此过程中新生链的结构至关重要。我们将环、α螺旋和β折叠中实际的氨基酸频率与在不存在对这些二级结构的任何氨基酸偏好情况下所出现的频率进行了比较。这项新分析表明，虽然存在特定氨基酸来驱动环和折叠片的形成，但没有一种氨基酸突出地作为α螺旋的驱动因素。这支持了这样一种观点，即α螺旋是大多数蛋白质在折叠过程开始之前的初始结构。
