The BICEP server models the linear increase in heat capacity of native proteins.
You can input a protein structure via a PDB identifier or upload a PDB-formatted file and optionally
provide experimental data on the heat capacity.
The output includes the calculated hydrophic surface area (HSA) and molecular weight
as well as the equation for the HSA baseline,
and a graph of the heat capacity baseline, optionally including the experimental data.
The hydrophobic residues in the structure are coloured in the protein and provided as static images as well as interactively via the
Jmol applet.
Requirements:
For optimal use, please enable Javascript. For using the optional Jmol applet, you need to have
any new web browser supporting the HTML5 canvas.
Documentation:
References:
van Dijk, E., Varilly, P., Knowles, T.P.J., Frenkel, D. and Abeln, S. (2016)
Consistent treatment of hydrophobicity in protein lattice models accounts for cold denaturation.
Physiscal Review Letters (accepted).
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