Bibliographic record
Abstract
The solution-phase association of biological molecules to form aggregates has been studied from a variety of perspectives, such as the flocculation of polymers, association of colloids and the aggregation of proteins. The latter subject has been the target of particular attention, mainly because of its importance in biomedical applications as well as its implication in diseases such as spongiform encephalopathies and Alzheimer's disease. Investigating protein aggregation at a fundamental level, however, is often complicated by the poorly defined structures of the aggregation products formed, as well as by the difficulty in working with biological systems. In this thesis, studies of Type-I collagen, a rod-like protein which can undergo 'in vitro' aggregation into highly-ordered protein structures, have been carried out with a view towards determining the mechanisms by which protein aggregates form. Two particular aggregate structures have been investigated. The first, a block-like aggregate called segmental long spacing collagen, was formed by the addition of nucleotide triphosphates to collagen monomers. By analyzing aggregate structures, formation kinetics and growth thermodynamics, it was concluded that these aggregates form via a hierarchical growth mechanism involving the formation of a stable intermediate and subsequent fusion of these intermediates. The second form of aggregate investigated was a fibril referred to as fibrous long spacing collagen. In this case, particular insight was made into elucidating the structure of these fibrils using the atomic force microscope. Results obtained again suggest that this aggregate forms via a hierarchical mechanism, first forming stable 'protofibrils', which then merge in a complex manner to produce the final structure. In the final Part of this thesis, the capabilities of the atomic force microscope in performing imaging of dynamic, biological processes in real time was examined, and was used to image the enzymatic digestion of collagen fibrils by the protein collagenase. The utility of the atomic force microscopy for 'in situ' investigation of complex processes such as collagen formation is discussed with a view towards applying this technique to future work.
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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 | 0.001 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.001 | 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".