%0 Journal Article
%T rediction of temperature factors from protein sequence
%A Shrihari Sonavane
%A Ashok A Jaybhaye
%A Ajaykumar G Jadhav
%J Bioinformation
%D 2013
%I 
%X Protein flexibility is useful in structural and functional aspect of proteins. We have analyzed the local primary protein sequence features that in combination can predict the B-value of amino acid residues directly from the protein sequence. We have also analyzed the distribution of B-value in different regions of protein three dimensional structures. On an average, the normalized B-value decreases by 0.1055 with every 0.5  increase in the distance of the residue from protein surface. The residues in the loop regions have higher B-values as compared to the residues present in other regular secondary structural elements. Buried residues which are present in the protein core are more rigid (lower B-values) than the residues present on the protein surface. Similarly, the hydrophobic residues which tend to be present in the protein core have lower average B-value than the polar residues. Finally, we have proposed the method based on Support Vector Regression (SVR) to predict the B-value from protein primary sequence. Our result shows that, the SVR model achieved the correlation coefficient of 0.47 which is comparable to existing methods.
%K B-value
%K Protein flexibility
%K Support Vector Regression
%K Sliding window approach
%K Protein dynamics.
%U http://www.bioinformation.net/009/97320630009134.pdf