PROFbval: predict flexible and rigid residues in proteins.

TitlePROFbval: predict flexible and rigid residues in proteins.
Publication TypeJournal Article
Year of Publication2006
AuthorsSchlessinger, A, Yachdav, G, Rost, B
Date Published2006 Apr 1
KeywordsComputational Biology, Databases, Protein, Protein Conformation, Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Software

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. AVAILABILITY: CONTACT: SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Alternate JournalBioinformatics
PubMed ID16455751
Grant ListR01-GM64633-01 / GM / NIGMS NIH HHS / United States
R01-LM07329 / LM / NLM NIH HHS / United States
R01-LM07329-01 / LM / NLM NIH HHS / United States