Folding and unfolding characteristics of short beta strand peptides under different environmental conditions and starting configurations

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• 作者：Astrid Maaß ; Emine Deniz Tekin ; Anton Schü ; ller ; Ahmet Palazoglu ; Dirk Reith ; Rol ; Faller
• 关键词：Protein folding ; Principal component analysis ; Beta strands
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2010
• 出版时间：October 2010
• 年：2010
• 卷：1804
• 期：10
• 页码：2003-2015
• 全文大小：3610 K

文摘

We analyze the effect of different environmental conditions, sequence lengths and starting configurations on the folding and unfolding pathways of small peptides exhibiting beta turns. We use chignolin and a sequence of peptide G as examples. A variety of different analysis tools allows us to characterize the changes in the folding pathways. It is observed that different harmonic modes dominate not only for different conditions but also for different starting points. The modes remain essentially very similar but their relative importance varies. A detailed analysis from diverse viewpoints including the influence of the particular amino acid sequence, conformational aspects as well as the associated motions yields a global picture that is consistent with experimental evidence and theoretical studies published elsewhere. Patterns of modes that remain stable over a range of temperatures might serve as an additional diagnostic to identify conformations that have reliably adopted a native fold. This could aid in reconstructing the folding process of a complete protein by identifying conformationally determined regions.