4ozb: Difference between revisions

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ozb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ozb RCSB], [http://www.ebi.ac.uk/pdbsum/4ozb PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

The thermodynamics of protein folding are dictated by a complex interplay of interatomic interactions and physical forces. A variety of unnatural protein-like oligomers have the capacity to manifest defined folding patterns. While the energetics of folding in natural proteins is well studied, little is known about the forces that govern folding in modified backbones. Here, we explore the thermodynamic consequences of backbone alteration on protein folding, focusing on two types of chemical changes made in different structural contexts of a compact tertiary fold. Our results reveal a surprising favorable impact on folding entropy that accompanies modifications that increase disorder in the ensemble of unfolded states, due to differences in the solvation of natural and unnatural backbones.

Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.,Reinert ZE, Horne WS Chem Sci. 2014 Aug 1;5(8):3325-3330. PMID:25071931<ref>PMID:25071931</ref>

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

</div>

== References ==

__TOC__

</StructureSection>

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 <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ozb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ozb RCSB], [http://www.ebi.ac.uk/pdbsum/4ozb PDBsum]</span></td></tr>
 <table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The thermodynamics of protein folding are dictated by a complex interplay of interatomic interactions and physical forces. A variety of unnatural protein-like oligomers have the capacity to manifest defined folding patterns. While the energetics of folding in natural proteins is well studied, little is known about the forces that govern folding in modified backbones. Here, we explore the thermodynamic consequences of backbone alteration on protein folding, focusing on two types of chemical changes made in different structural contexts of a compact tertiary fold. Our results reveal a surprising favorable impact on folding entropy that accompanies modifications that increase disorder in the ensemble of unfolded states, due to differences in the solvation of natural and unnatural backbones.
+Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.,Reinert ZE, Horne WS Chem Sci. 2014 Aug 1;5(8):3325-3330. PMID:25071931<ref>PMID:25071931</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>