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S. A. Woodson

Publications and source records attributed to S. A. Woodson.

2 recordsLinked to original sources

Persistence Length Changes Dramatically as RNA Folds

We determine the persistence length, $l_p$, for a bacterial group I ribozyme as a function of concentration of monovalent and divalent cations by fitting the distance distribution functions $P(r)$ obtained from small angle X-ray scattering intensity data to the asymptotic form of the calculated $P_{WLC}(r)$ for a worm-like chain (WLC). The $l_p$ values change dramatically over a narrow range of \Mg concentration from $\sim$21 Åin the unfolded state (\textbf{U}) to $\sim$10 Åin the compact ($\mathrm{I_C}$) and native states. Variations in $l_p$ with increasing \Na concentration are more gradual. In accord with the predictions of polyelectrolyte theory we find $l_p \propto 1/ κ^2$ where $κ$ is the inverse Debye-screening length.

q-bio.BM↗

Kinetic Partitioning Mechanism as a Unifying Theme in the Folding of Biomolecules

We present a unified framework for folding kinetics of proteins and RNA. The basis for this framework relies on the notion of topological frustration, which gives rise to several competing basins of attraction (CBA) in addition to the native basin of attraction (NBA) on the free energy surface. A rough free energy surface results in direct and indirect pathways to the NBA, i.e., a kinetic partitioning mechanism (KPM). The unified framework for folding kinetics allows us to propose a foldability principle, according to which fast folding sequences are characterized by the folding transition temperature $T_{F}$ being close to the collapse transition temperature $T_{θ}$. Biomolecules, for which foldability principle is satisfied, such as small proteins and tRNAs, are expected to fold rapidly with two-state kinetics. Estimates for the multiple time scales in KPM are also given.

cond-mat.soft↗