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Structural and cell biology studies often require engineering proteins with enhanced solubility.
This server identifies solvent exposed hydrophobic residues in a protein sequence,
and compares them with those of closely related sequences, providing thus useful help to select
the best residues to be targeted for site-directed mutagenesis.
Note: Altering solvent exposed surface residues can result in loss
of the biological function of a protein. Therefore, the information generated by this tool should
be complemented with any available experimental data.
These are the steps followed by the server:
1. Models the 3D-structure the of input sequence (query). Models are produced by
SCWRL, using a template obtained from a PSI-BLAST search against the PDB database.
Model is only built only if the e-value of the sequence template is < 1e-5.
If the template identity to the query is > 95% following calculations are carried out
over the template. Insertions and deletions are not modeled in this version of the program
2. Calculates the Fractional Solvent accessibility of the models using NACCESS
3. Outputs a 3D-model of the query, and a multiple
sequence alignment of the query and various close orthologues.