- Rossi, Paolo;
- Shi, Lei;
- Liu, Gaohua;
- Barbieri, Christopher M;
- Lee, Hsiau‐Wei;
- Grant, Thomas D;
- Luft, Joseph R;
- Xiao, Rong;
- Acton, Thomas B;
- Snell, Edward H;
- Montelione, Gaetano T;
- Baker, David;
- Lange, Oliver F;
- Sgourakis, Nikolaos G
Oligomeric proteins are important targets for structure determination in solution. While in most cases the fold of individual subunits can be determined experimentally, or predicted by homology-based methods, protein-protein interfaces are challenging to determine de novo using conventional NMR structure determination protocols. Here we focus on a member of the bet-V1 superfamily, Aha1 from Colwellia psychrerythraea. This family displays a broad range of crystallographic interfaces none of which can be reconciled with the NMR and SAXS data collected for Aha1. Unlike conventional methods relying on a dense network of experimental restraints, the sparse data are used to limit conformational search during optimization of a physically realistic energy function. This work highlights a new approach for studying minor conformational changes due to structural plasticity within a single dimeric interface in solution.