Effect of Weakly Interacting Cosolutes on Lysozyme Conformations
| Autor: | Roi Asor, Asaf Shemesh, Uri Raviv, Yehonatan Levartovsky |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Quantitative Biology::Biomolecules Scattering General Chemical Engineering A protein Thermodynamics General Chemistry 010402 general chemistry Elastic network Contact model 01 natural sciences Article 0104 chemical sciences lcsh:Chemistry 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology lcsh:QD1-999 chemistry Normal mode ddc:660 Denaturation (biochemistry) Lysozyme Guanidine |
| Zdroj: | ACS omega 3(11), 16246-16252 (2018). doi:10.1021/acsomega.8b01289 ACS Omega ACS Omega, Vol 3, Iss 11, Pp 16246-16252 (2018) |
| ISSN: | 2470-1343 |
| Popis: | ACS omega 3(11), 16246 - 16252 (2018). doi:10.1021/acsomega.8b01289 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. Published by ACS Publications, Washington, DC |
| Databáze: | OpenAIRE |
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