Literature DB >> 17270497

Hidden symmetries in the primary sequences of beta-barrel family.

Xiaofeng Ji1, Hanlin Chen, Yi Xiao.   

Abstract

In this paper, we analyze the symmetries of beta-barrel proteins at both structure and sequence levels by using a modified recurrent quantification analysis. It shows that the structures and sequences have the same two-fold symmetry, although the later diverged considerably. This result may be helpful to understand the mechanism of protein evolution.

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Year:  2007        PMID: 17270497     DOI: 10.1016/j.compbiolchem.2007.01.002

Source DB:  PubMed          Journal:  Comput Biol Chem        ISSN: 1476-9271            Impact factor:   2.877


  2 in total

1.  Symmetric key structural residues in symmetric proteins with beta-trefoil fold.

Authors:  Jianhui Feng; Mingfeng Li; Yanzhao Huang; Yi Xiao
Journal:  PLoS One       Date:  2010-11-30       Impact factor: 3.240

2.  How the Sequence of a Gene Specifies Structural Symmetry in Proteins.

Authors:  Xiaojuan Shen; Tongcheng Huang; Guanyu Wang; Guanglin Li
Journal:  PLoS One       Date:  2015-12-07       Impact factor: 3.240

  2 in total

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