PROFbval: Predict flexible and rigid residues in proteins

Avner Schlessinger, Guy Yachdav, Burkhard Rost

Research output: Contribution to journalArticlepeer-review

127 Scopus citations


Summary: The mobility of a residue on the protein surface is closely linked to its function. The identification of extremely rigid or flexible surface residues can therefore contribute information crucial for solving the complex problem of identifying functionally important residues in proteins. Mobility is commonly measured by B-value data from high-resolution three-dimensional X-ray structures. Few methods predict B-values from sequence. Here, we present PROFbval, the first web server to predict normalized B-values from amino acid sequence. The server handles amino acid sequences (or alignments) as input and outputs normalized B-value and two-state (flexible/rigid) predictions. The server also assigns a reliability index for each prediction. For example, PROFbval correctly identifies residues in active sites on the surface of enzymes as particularly rigid.

Original languageEnglish
Pages (from-to)891-893
Number of pages3
Issue number7
StatePublished - 1 Apr 2006
Externally publishedYes


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