Name
Abstract | ||
|---|---|---|
Hydrophobins, produced by filamentous fungi, are small amphipathic proteins whose biological functions rely on their unique surface-activity properties. Understanding the mechanistic details of themultimerization process is of primary importance to clarify the interfacial activity of hydrophobins. We used free energy calculations to study the role of a flexible beta-hairpin in the multimerization process in hydrophobin II from Trichoderma reesei (HFBI). We characterized how the displacement of this beta-hairpin controls the stability of the monomers/dimers/ tetramers in solution. The regulation of the oligomerization equilibrium of HFBI will necessarily affect its interfacial properties, fundamental for its biological function and for technological applications. Moreover, we propose possible routes for the multimerization process of HFBI in solution. This is the first case where a mechanism by which a flexible loop flanking a rigid patch controls the protein-protein binding equilibrium, already known for proteins with charged binding hot-spots, is described within a hydrophobic patch. |
Year | DOI | Venue |
|---|---|---|
2016 | 10.1371/journal.pcbi.1005202 | PLOS COMPUTATIONAL BIOLOGY |
Field | DocType | Volume |
Plasma protein binding,Protein multimerization,Binding site,Biology,Biochemistry,Fungal protein,Trichoderma,Genetics,Protein structure | Journal | 12 |
Issue | Citations | PageRank |
11 | 0 | 0.34 |
References | Authors | |
4 | 2 | |
Name | Order | Citations | PageRank |
|---|---|---|---|
| Laura Riccardi | 1 | 0 | 0.34 |
| Paolo Mereghetti | 2 | 182 | 8.61 |