| Summary: | 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 Bvalue
decreases by 0.1055 with every 0.5Å 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.
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