Effect of Weakly Interacting Cosolutes on Lysozyme Conformations

Yehonatan Levartovsky, Asaf Shemesh, Roi Asor, Uri Raviv*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Exposure of a protein to cosolutes, like denaturants, changes its folding equilibrium. To determine the ensemble of protein conformations at equilibrium, in the presence of weakly interacting cosolutes, we present a two-stage analysis of solution X-ray scattering data. In the first stage, Guinier analysis and Kratky plot revealed information about the compactness and flexibility of the protein. In the second stage, elastic network contact model and coarse-grained normal mode analysis were used to generate an ensemble of conformations. The scattering curves of the conformations were computed and fitted to the measured scattering curves to get insights into the dominating folding states at equilibrium. Urea and guanidine hydrochloride (GuHCl) behaved as preferentially included weakly interacting cosolutes and induced denaturation of hen egg-white lysozyme, which served as our test case. The computed models adequately fit the data and gave ensembles of conformations that were consistent with our measurements. The analysis suggests that in the presence of urea, lysozyme retained its compactness and assumed molten globule characteristics, whereas in the presence of GuHCl lysozyme adopted random coiled conformations. Interestingly, no equilibrium intermediate states were observed in both urea and GuHCl.

Original languageAmerican English
Pages (from-to)16246-16252
Number of pages7
JournalACS Omega
Issue number11
StatePublished - 29 Nov 2018

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Copyright © 2018 American Chemical Society.


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