View source for 7tir


==Backbone-modified variant of the B domain of Staphylococcal protein A: beta3-residues in helix 3==
<StructureSection load='7tir' size='340' side='right'caption='[[7tir]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7tir]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TIR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3A:(3S)-3-AMINOBUTANOIC+ACID'>B3A</scene>, <scene name='pdbligand=B3E:(3S)-3-AMINOHEXANEDIOIC+ACID'>B3E</scene>, <scene name='pdbligand=B3K:(3S)-3,7-DIAMINOHEPTANOIC+ACID'>B3K</scene>, <scene name='pdbligand=B3X:(3S)-3,5-DIAMINO-5-OXOPENTANOIC+ACID'>B3X</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7tir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tir OCA], [https://pdbe.org/7tir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tir RCSB], [https://www.ebi.ac.uk/pdbsum/7tir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tir ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2UW47_STAAU Q2UW47_STAAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sequence-encoded folding is the foundation of protein structure and is also possible in synthetic chains of artificial chemical composition. In natural proteins, the characteristics of the unfolded state are as important as those of the folded state in determining folding energetics. While much is known about folded structures adopted by artificial protein-like chains, corresponding information about the unfolded states of these molecules is lacking. Here, we report the consequences of altered backbone composition on the structure, stability, and dynamics of the folded and unfolded states of a compact helix-rich protein. Characterization through a combination of biophysical experiments and atomistic simulation reveals effects of backbone modification that depend on both the type of artificial monomers employed and where they are applied in sequence. In general, introducing artificial connectivity in a way that reinforces characteristics of the unfolded state ensemble of the prototype natural protein minimizes the impact of chemical changes on folded stability. These findings have implications in the design of protein mimetics and provide an atomically detailed picture of the unfolded state of a natural protein and artificial analogues under non-denaturing conditions.

Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.,Santhouse JR, Leung JMG, Chong LT, Horne WS Chem Sci. 2022 Sep 20;13(40):11798-11806. doi: 10.1039/d2sc04427g. eCollection , 2022 Oct 19. PMID:36320921<ref>PMID:36320921</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7tir" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Chong LT]]
[[Category: Horne WS]]
[[Category: Leung JMG]]
[[Category: Santhouse JR]]