6d37 | pdb_00006d37

Trp-cage tr16b R16Nva : Elimination of pH Dependent Interactions

spinqualitylabelsall models 6d37 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6d37 is a 1 chain structure with sequence from Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 32 models Ligands: ACE, DAL, NH2, NVA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The Trp-cage, an 18-20 residue miniprotein, has emerged as a primary test system for evaluating computational fold prediction and folding rate determination efforts. As it turns out, a number of stabilizing interactions in the Trp-cage folded state have a strong pH dependence; all prior Trp-cage mutants have been destabilized under carboxylate-protonating conditions. Notable among the pH dependent stabilizing interactions within the Trp-cage are: (1) an Asp as the helix N-cap, (2) an H-bonded Asp9/Arg16 salt bridge, (3) an interaction between the chain termini which are in close spatial proximity, and (4) additional side chain interactions with Asp9. In the present study, we have prepared Trp-cage species that are significantly more stable at pH 2.5 (rather than 7) and quantitated the contribution of each interaction listed above. The Trp-cage structure remains constant with the pH change. The study has also provided measures of the stabilizing contribution of indole ring shielding from surface exposure and the destabilizing effects of an ionized Asp at the C-terminus of an alpha-helix. Reversing the typical pH stability profile of the Trp-cage.,Graham KA, Byrne A, Son R, Andersen NH Biopolymers. 2019 Mar;110(3):e23260. doi: 10.1002/bip.23260. Epub 2019 Feb 19. PMID:30779444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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