Extended Law of Corresponding States Applied to Solvent Isotope Effect on a Globular Protein
(2016) In The Journal of Physical Chemistry Letters 7(9). p.1610-1615- Abstract
- Investigating proteins with techniques such as NMR or neutron scattering frequently requires the partial or complete substitution of D2O for H2O as a solvent, often tacitly assuming that such a solvent substitution does not significantly alter the properties of the protein. Here, we report a systematic investigation of the solvent isotope effect on the phase diagram of the lens protein gamma B-crystallin in aqueous solution as a model system exhibiting liquid-liquid phase separation. We demonstrate that the observed strong variation of the critical temperature T-c can be described by the extended law of corresponding states for all H2O/D2O ratios, where scaling of the temperature by T-c or the reduced second virial coefficient accurately... (More)
- Investigating proteins with techniques such as NMR or neutron scattering frequently requires the partial or complete substitution of D2O for H2O as a solvent, often tacitly assuming that such a solvent substitution does not significantly alter the properties of the protein. Here, we report a systematic investigation of the solvent isotope effect on the phase diagram of the lens protein gamma B-crystallin in aqueous solution as a model system exhibiting liquid-liquid phase separation. We demonstrate that the observed strong variation of the critical temperature T-c can be described by the extended law of corresponding states for all H2O/D2O ratios, where scaling of the temperature by T-c or the reduced second virial coefficient accurately reproduces the binodal, spinodal, and osmotic compressibility. These findings highlight the impact of H2O/D2O substitution on gamma B-crystallin properties and warrant further investigations into the universality of this phenomenon and its underlying mechanisms. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/78a0b6ef-5aab-4e82-856f-e76cf024346b
- author
- BUCCIARELLI, SASKIA LU ; Mahmoudi, Najet LU ; Casal-Dujat, Lucia LU ; Jehannin, Marie ; Jud, Corinne and Stradner, Anna LU
- organization
- publishing date
- 2016-05-05
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of Physical Chemistry Letters
- volume
- 7
- issue
- 9
- pages
- 6 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:27077243
- scopus:84968754943
- wos:000375638500002
- ISSN
- 1948-7185
- DOI
- 10.1021/acs.jpclett.6b00593
- language
- English
- LU publication?
- yes
- id
- 78a0b6ef-5aab-4e82-856f-e76cf024346b
- alternative location
- http://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.6b00593
- date added to LUP
- 2016-10-25 16:13:03
- date last changed
- 2022-04-24 18:31:55
@article{78a0b6ef-5aab-4e82-856f-e76cf024346b, abstract = {{Investigating proteins with techniques such as NMR or neutron scattering frequently requires the partial or complete substitution of D2O for H2O as a solvent, often tacitly assuming that such a solvent substitution does not significantly alter the properties of the protein. Here, we report a systematic investigation of the solvent isotope effect on the phase diagram of the lens protein gamma B-crystallin in aqueous solution as a model system exhibiting liquid-liquid phase separation. We demonstrate that the observed strong variation of the critical temperature T-c can be described by the extended law of corresponding states for all H2O/D2O ratios, where scaling of the temperature by T-c or the reduced second virial coefficient accurately reproduces the binodal, spinodal, and osmotic compressibility. These findings highlight the impact of H2O/D2O substitution on gamma B-crystallin properties and warrant further investigations into the universality of this phenomenon and its underlying mechanisms.}}, author = {{BUCCIARELLI, SASKIA and Mahmoudi, Najet and Casal-Dujat, Lucia and Jehannin, Marie and Jud, Corinne and Stradner, Anna}}, issn = {{1948-7185}}, language = {{eng}}, month = {{05}}, number = {{9}}, pages = {{1610--1615}}, publisher = {{The American Chemical Society (ACS)}}, series = {{The Journal of Physical Chemistry Letters}}, title = {{Extended Law of Corresponding States Applied to Solvent Isotope Effect on a Globular Protein}}, url = {{http://dx.doi.org/10.1021/acs.jpclett.6b00593}}, doi = {{10.1021/acs.jpclett.6b00593}}, volume = {{7}}, year = {{2016}}, }