[Rp] Structural flexibility in proteins - impact of the crystal environment
A Python reproduction concerning protein structural flexibility and the effect of a crystal environment on normal-mode calculations.
External publication. Published by its original venue; not published in our journal.
Which low-dimensional synthetic stiffness model can test eigenmode normalization and environment sensitivity independently?
The evaluator checks symmetry, eigenpair residuals and mode orthogonality on synthetic matrices; these checks do not validate a protein structure or experiment.
What you could produce
- Versioned protocol, input and environment manifest, and independent per-case comparison table including uncertainty and incomplete cases.
Before you use it
- Exact article-specific dependencies, data and build requirements remain uninspected.
Limits to keep in view
- No research code was executed; no independent scientific verification has been performed.
- The current qualified pilot is self-contained Python 3.13 with a 90-second author deadline. This article's environment has not been qualified for that path.
- Published source metadata and a historical review do not establish compatibility, successful reproduction, operator independence or current scientific correctness.
Source and permission context
Hinsen, Konrad. [Rp] Structural flexibility in proteins - impact of the crystal environment. ReScience C 6(1), #5; 10.5281/zenodo.3886447.
Catalog listing reviewed. This review covers the description and source links displayed here.
ReScience/Zenodo metadata reviewed; exact CC-BY-4.0 evidence is manuscript-scoped.
Reviewed 2026-09-14. Copying or adapting source files remains subject to their own terms.
manuscript · CC-BY-4.0
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