Self-avoiding walk
The self-avoiding walk (SAW), exposed through SAW, models a
chain in a good solvent, where excluded-volume interactions swell the chain relative to an
ideal coil. It uses the universal end-to-end distribution form of des Cloizeaux as
implemented by O’Brien et al. (2009), at the fixed good-solvent scaling exponent
\(\nu \approx 0.588\). It is composition-independent.
Mathematical formalism
The end-to-end distribution is the scaling form
with the small-\(r\) exponent \(\theta = 0.3\), the large-\(r\) exponent \(\delta = 2.5\), normalisation constants \(a = 3.679\), \(b = 1.232\), and a chain-length-dependent scale
The radius of gyration is obtained from the end-to-end size via the universal ratio
Parameters
Parameter |
Default |
Meaning and typical values |
|---|---|---|
|
5.5 Å |
Sets the absolute per-monomer length scale in \(R_{ee} = \texttt{prefactor}\,N^{0.598}\). Values around 5-6 Å are reasonable, but the prefactor should be tuned to match explicit excluded-volume simulations for quantitative work. |
The scaling exponent is fixed at the good-solvent value (\(\nu \approx 0.588\)). To vary \(\nu\) continuously, use the nu-dependent SAW instead.
What to expect for a protein. Because \(\nu \approx 0.6 > 0.5\), the SAW is more expanded than the AFRC and is an appropriate reference for a strongly solvated, expanded IDR. The prefactor sets where the absolute dimensions land; with a value near 5.5 Å the SAW gives end-to-end and \(R_g\) values noticeably larger than the theta-state AFRC.
Citations
O’Brien, E. P., Morrison, G., Brooks, B. R., & Thirumalai, D. (2009). How accurate are polymer models in the analysis of Förster resonance energy transfer experiments on proteins? The Journal of Chemical Physics, 130(12), 124903.
des Cloizeaux, J. (1974). Lagrangian theory for a self-avoiding random chain. Physical Review A, 10(5), 1665-1669.