Project name: dyn_full_ser [mutate: CA377S, CA387S, CA406S, CA416S]

Status: running

submitted: 2018-03-12 12:16:15, status changed: 2018-03-12 12:20:13
Settings
Chain sequence(s) A: NSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPCTDLFKRYQQCVQKAI
Distance of aggregation 10 Å
Dynamic mode Yes
Mutated residues CA377S, CA387S, CA406S, CA416S
Energy difference between WT (input) and mutated protein (by FoldX) None kcal/mol

Changes in protein stability upon mutation are calculated using the FoldX forcefield. Computational prediction of protein stability is used with the intention of preventing the experimental characterization of proteins bearing mutations that significantly destabilize their structure. Mutations resulting in a predicted reduction in protein stability ≥ 1 kcal/mol are considered disruptive.


 

Laboratory of Theory of Biopolymers 2015