4xcr: Difference between revisions

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== Function ==

[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

== Publication Abstract from PubMed ==

Although protein folding and stability have been well explored under simplified conditions in vitro, it is yet unclear how these basic self-organization events are modulated by the crowded interior of live cells. To find out, we use here in-cell NMR to follow at atomic resolution the thermal unfolding of a beta-barrel protein inside mammalian and bacterial cells. Challenging the view from in vitro crowding effects, we find that the cells destabilize the protein at 37 degrees C but with a conspicuous twist: While the melting temperature goes down the cold unfolding moves into the physiological regime, coupled to an augmented heat-capacity change. The effect seems induced by transient, sequence-specific, interactions with the cellular components, acting preferentially on the unfolded ensemble. This points to a model where the in vivo influence on protein behavior is case specific, determined by the individual protein's interplay with the functionally optimized "interaction landscape" of the cellular interior.

Thermodynamics of protein destabilization in live cells.,Danielsson J, Mu X, Lang L, Wang H, Binolfi A, Theillet FX, Bekei B, Logan DT, Selenko P, Wennerstrom H, Oliveberg M Proc Natl Acad Sci U S A. 2015 Oct 6;112(40):12402-7. doi:, 10.1073/pnas.1511308112. Epub 2015 Sep 21. PMID:26392565<ref>PMID:26392565</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Superoxide Dismutase|Superoxide Dismutase]]

== References ==

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@@ Line 12: / Line 12: @@
 == Function ==
 [[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Although protein folding and stability have been well explored under simplified conditions in vitro, it is yet unclear how these basic self-organization events are modulated by the crowded interior of live cells. To find out, we use here in-cell NMR to follow at atomic resolution the thermal unfolding of a beta-barrel protein inside mammalian and bacterial cells. Challenging the view from in vitro crowding effects, we find that the cells destabilize the protein at 37 degrees C but with a conspicuous twist: While the melting temperature goes down the cold unfolding moves into the physiological regime, coupled to an augmented heat-capacity change. The effect seems induced by transient, sequence-specific, interactions with the cellular components, acting preferentially on the unfolded ensemble. This points to a model where the in vivo influence on protein behavior is case specific, determined by the individual protein's interplay with the functionally optimized "interaction landscape" of the cellular interior.
+Thermodynamics of protein destabilization in live cells.,Danielsson J, Mu X, Lang L, Wang H, Binolfi A, Theillet FX, Bekei B, Logan DT, Selenko P, Wennerstrom H, Oliveberg M Proc Natl Acad Sci U S A. 2015 Oct 6;112(40):12402-7. doi:, 10.1073/pnas.1511308112. Epub 2015 Sep 21. PMID:26392565<ref>PMID:26392565</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4xcr" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Superoxide Dismutase|Superoxide Dismutase]]
 == References ==
 <references/>