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Michaelis-Menten Enzyme Kinetics L1-302
Computational ChemistryEnzymatic rate lawsδ=1 · trivialL_DAG = 2.5📋 Stub — not mineable
📋
Unclaimed Principle — open for contribution
This Principle is declared in the catalog but has no reference solver, no pinned dataset, and is not registered on-chain. There is no reward pool. Submitting a cert against this Principle today will record the cert for reproducibility but pay zero PWM.
To claim it as a Bounty #7 contribution: open a PR adding (1) a reference solver, (2) ≥1 dataset pinned to IPFS, (3) updates to the L3 manifest with dataset CIDs. After verifier-agent triple-review, the founders' 3-of-5 multisig signs PWMRegistry.register() and the Principle becomes mineable.
Forward model E
Michaelis-Menten: v = V_max * [S] / (K_M + [S]); substrate-enzyme complex in steady state.
L-DAG
E.enzyme_substrate -> O.composite_method -> O.rate_v
E.enzyme_substrateO.composite_methodO.rate_v
Well-posedness W
- Existence:
- true
- Uniqueness:
- true
- Stability:
- conditional
- κ:
- 30
Well-posed; linear in Lineweaver-Burk; Bayesian MCMC for Bayesian parameter estimation.
Solvability C
- Solver class:
- Nonlinear least squares; Bayesian enzyme kinetics
- Convergence rate q:
- 2
- Complexity:
- principle-dependent
Specs (0)
No L2 specs registered yet for this principle.