PROFbval: predict flexible and rigid residues in proteins.
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.


BACKGROUND
http://www.rostlab.org/services/profbval


BACKGROUND
profbval@rostlab.org


BACKGROUND
Supplementary data are available at Bioinformatics online.
Schlessinger
Avner
A
CUBIC, Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street BB217, New York, NY 10032, USA. profbval@rostlab.org
Yachdav
Guy
G
Rost
Burkhard
B
D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment / Q000379:methods; D017386:Sequence Homology, Amino Acid; D012984:Software
D011506:Proteins