SSIPe is a method to calculate binding affinity changes
(ΔΔGbind) of protein-protein interactions (PPIs)
upon mutations at protein-protein interface.
Starting from a PPI complex structure, SSPIe first generates
multple structure and sequence alignments from
STRING databases separately.
The structural and sequence profiles are then combined with
the physical energy function
to predict the impact of the mutations on PPI binding free energies.
When a mutation does not take place at the interface, only the
EvoEF force field
will be used to predict the binding affinity change.
SSIPe can be used to guide the designing and engineering of
protein-protein interactions with enhanced binding affinity, and/or
for understanding the roles of disease-related mutations
associated with protein-protein interactions. The SSIPe server is developed
to handel the cases where a mutation is only involved in a dimer. If users
want to calculate the binding affinity change caused by a mutation in a
multimer (multi-chain) protein, they can use the 'ComputeBinding' module of the
EvoEF program coupling
with the 'split' option.
(>> Read more about SSIPe).
Please direct questions and inquiries to our Service System Discussion Board or contact Dr. Xiaoqiang Huang.
yangzhanglabumich.edu | (734) 647-1549 | 100 Washtenaw Avenue, Ann Arbor, MI 48109-2218