Journal
BIOINFORMATICS
Volume 22, Issue 7, Pages 891-893Publisher
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/btl032
Keywords
-
Categories
Funding
- NIGMS NIH HHS [R01-GM64633-01] Funding Source: Medline
- NLM NIH HHS [R01-LM07329, R01-LM07329-01] Funding Source: Medline
Ask authors/readers for more resources
Summ.: 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available