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The flexibility state of a residue is frequently correlated with the flexibility states of its neighbors.

B-factors (also referred to as B-values, Debye-Waller factors, or temperature factors) reported in experimentally determined protein structures are commonly used to represent protein flexibility and its local mobility [Although each atom in protein atomic resolution structures has its B-factor, the B-factor of the whole residue is generally represented by its Cα B-factor.

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This flexibility of protein structures is associated with various biological processes.


Predicting flexibility of residues from protein sequences is significant for analyzing the dynamic properties of proteins which will be helpful in predicting their functions.

The method incorporates sequence and evolutionary information, context-based scores, predicted secondary structures and solvent accessibility, and amino acid properties.


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