6z35

De-novo Maquette 2 protein with buried ion-pair

spinqualitylabelsall models 6z35 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Soluble proteins are universally packed with a hydrophobic core and a polar surface that drive the protein folding process. Yet charged networks within the central protein core are often indispensable for the biological function. Here, we show that natural buried ion-pairs are stabilised by amphiphilic residues that electrostatically shield the charged motif from its surroundings to gain structural stability. To explore this effect, we build artificial proteins with buried ion-pairs by combining directed computational design and biophysical experiments. Our findings illustrate how perturbation in charged networks can introduce structural rearrangements to compensate for desolvation effects. We validate the physical principles by resolving high-resolution atomic structures of the artificial proteins that are resistant towards unfolding at extreme temperatures and harsh chemical conditions. Our findings provide a molecular understanding of functional charged networks and how point mutations may alter the protein's conformational landscape. Design of buried charged networks in artificial proteins.,Baumgart M, Ropke M, Muhlbauer ME, Asami S, Mader SL, Fredriksson K, Groll M, Gamiz-Hernandez AP, Kaila VRI Nat Commun. 2021 Mar 25;12(1):1895. doi: 10.1038/s41467-021-21909-7. PMID:33767131 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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