Searching for functions of a particular gene has always remained a question of importance. Site- directed mutagenesis has always served as  a tool for such such kind of analysis. With the accumulation of sequence data, it has become easy to do such kind of mutation studies in-silico. Cang Z. et al. (2017) have recently introduced such an in-silico approach which has advantages over conventional site- directed mutagenesis.

       They have used topology based homology methods to determine the degrees of freedom of the changed protein. The new method has proved useful than the existing methods in predicting functions of  globular proteins. They have also calculated pearson correlated coefficient for changed proteins. They have carried out the analysis on membrane globular proteins

     The implementation of the analysis can be visualized at the following URL: http://weilab.math.msu.edu/TML/TML-MP/

Refrence:

Cang Z. et al. (2017) Analysis and prediction of protein folding energy changes upon mutation by element specific persistent homology. Bioinformatics 33(22): 3549-3557.


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