A novel molecular dynamics approach to evaluate the effect of phosphorylation on multimeric protein interface: the αB-Crystallin case study
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- 作者：Federica Chiappori ; Luca Mattiazzi ; Luciano Milanesi ; Ivan Merelli
- 关键词：Post ; translational modification ; Phosphorylation ; Molecular dynamics ; PCA ; Clustering ; αB ; Crystallin ; Chaperone ; Small HSP
- 刊名：BMC Bioinformatics
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：17
- 期：4-supp
- 全文大小：2,354 KB
- 刊物主题：Bioinformatics; Microarrays; Computational Biology/Bioinformatics; Computer Appl. in Life Sciences; Combinatorial Libraries; Algorithms;
- 出版者：BioMed Central
- ISSN：1471-2105
文摘
Background Phosphorylation is one of the most important post-translational modifications (PTM) employed by cells to regulate several cellular processes. Studying the effects of phosphorylations on protein structures allows to investigate the modulation mechanisms of several proteins including chaperones, like the small HSPs, which display different multimeric structures according to the phosphorylation of a few serine residues. In this context, the proposed study is aimed at finding a method to correlate different PTM patterns (in particular phosphorylations at the monomers interface of multimeric complexes) with the dynamic behaviour of the complex, using physicochemical parameters derived from molecular dynamics simulations in the timescale of nanoseconds.