View source for 9bb1


==Backbone Modification in the GA Module of Protein PAB: Wild-type Sequence==
<StructureSection load='9bb1' size='340' side='right'caption='[[9bb1]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bb1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BB1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=9bb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bb1 OCA], [https://pdbe.org/9bb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bb1 RCSB], [https://www.ebi.ac.uk/pdbsum/9bb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bb1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAB_FINMA PAB_FINMA] Binds serum albumin.
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== Publication Abstract from PubMed ==
Targeted protein backbone modification can recreate tertiary structures reminiscent of folds found in nature on artificial scaffolds with improved biostability. Incorporation of altered monomers in such entities is typically limited to sites distant from the hydrophobic core to avoid potential disruptions to folding. This is limiting, as it is advantageous in some applications to incorporate artificial connectivity at buried sites. Here, we report an examination of protein backbone modification targeted specifically to hydrophobic core positions and its impacts on tertiary folded structure and fold stability. Different artificial monomer types are placed at core, core-flanking, or solvent-exposed positions in a compact three-helix protein. Effects on structure and folding energetics are assessed by NMR spectroscopy and biophysical methods. Results show that artificial residues can be well accommodated in the hydrophobic core of a defined tertiary fold, with effects on stability only modestly larger than identical changes at solvent-exposed sites. Collectively, these results provide new insights into folding behavior of protein-like artificial chains as well as strategies for the design of such molecules.

Backbone Modification in a Protein Hydrophobic Core.,Lin Y, Horne WS Chemistry. 2024 May 16:e202401890. doi: 10.1002/chem.202401890. PMID:38753977<ref>PMID:38753977</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9bb1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Finegoldia magna]]
[[Category: Large Structures]]
[[Category: Horne WS]]
[[Category: Lin Y]]