profbval 1.0.22-1 source package in Ubuntu
Changelog
profbval (1.0.22-1) unstable; urgency=low * Initial release in Debian (Closes: #680140) -- Laszlo Kajan <email address hidden> Tue, 14 Aug 2012 13:30:13 +0200
Upload details
- Uploaded by:
- Debian Med
- Uploaded to:
- Sid
- Original maintainer:
- Debian Med
- Architectures:
- all
- Section:
- misc
- Urgency:
- Low Urgency
See full publishing history Publishing
| Series | Published | Component | Section | |
|---|---|---|---|---|
| Trusty | release | universe | misc |
Downloads
| File | Size | SHA-256 Checksum |
|---|---|---|
| profbval_1.0.22-1.dsc | 1.4 KiB | 07643ffe7f6aa97343095e908ecc2d0fa00cd3dae1d5a2536969f63ca08ee5b0 |
| profbval_1.0.22.orig.tar.gz | 142.2 KiB | 4651a721ec20735daf9e87c727f742b301b38572f6e2146cb70f55bfdc088d8e |
| profbval_1.0.22-1.debian.tar.gz | 3.4 KiB | b5714dca76a21909d1afa9bb13aaa002ad31ce7db847ac33769a1dee4484402a |
No changes file available.
Binary packages built by this source
- profbval: predictor of flexible/rigid protein residues from sequence
PROFbval can be useful for both protein structure and
function predictions. For instance, a biologist can locate potentially
antigenic determinants by identifying the most flexible residues on the
protein surface. Additionally, a crystallographer can locate residues that
potentially have high experimental B-values.
.
PROFbval takes the following input, further described on profbval(1):
* a protein sequence in a FASTA file
* secondary structure and solvent accessibility prediction by prof(1)
* an HSSP file
.
Background: the mobility of a given residue on the protein surface is related
to its functional role.
Therefore, identification of extremely rigid or flexible
residues on the protein surface is helpful for identifying functionally
important residues in proteins. A common measure of atom mobility in proteins
is B-value data from x-ray crystallography structures. PROFbval is the first
tool to predict normalized backbone B-values from amino-acid sequence.
