Exploring the Structural Stability and Assembly Mechanism of Hydrophobin Proteins
Bibliographic record
Abstract
Hydrophobins are small, globular proteins with amphiphilic character that are produced and secreted by filamentous fungi. At hydrophobic‐hydrophilic interfaces they self‐assemble into durable amyloid‐containing structures, called rodlets, which create protective, water repellent coatings for fungal spores. Current models of hydrophobin self‐assembly predict that hydrophobin monomers undergo a conformational change at a hydrophobic‐hydrophilic interface and integrate into a growing rodlet, however the mechanistic details of rodlet assembly are unknown. To investigate the assembly mechanism of hydrophobins, we carried out stability studies with SC16, a hydrophobin isolated from Schizophyllum commune. SC16 was recombinantly expressed using E. coli and purified by immobilized Ni 2+ affinity chromatography. NMR spectroscopy was used to determine that the structure of SC16 was minimally perturbed by denaturing (8 M urea) or reducing (2 mM DTT) conditions. Gel filtration chromatography indicated that in solution SC16 exists as a tetramer, suggesting that rodlet assembly does not initiate from hydrophobin monomers. Mutant forms of SC16 are being employed to determine the sequences and conformational changes required for rodlet assembly, with gel filtration chromatography used to determine the multimeric state, thioflavin T assays to quantify amyloid formation, and electron microscopy to visualize rodlet formation. X‐ray crystallography is being used to further characterize the tetrameric structure of SC16. Determining which hydrophobin sequences are responsible for self‐assembly will allow the rational modification of hydrophobins to add new functionalities or influence their self‐assembly. Support or Funding Information NSERC, Dalhousie University Faculty of Medicine, Nova Scotia Research Foundation, BioActives CREATE
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How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.000 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".