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Metal-Binding protein - Europe PMC

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Last Updated: 16 January 2022

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Metal Ion Binding Induces Local Protein Unfolding and Destabilizes Human Carbonic Anhydrase II.

Anhydrase II, a robust metalloprotein and a robust biological model system for investigating metal ion coordination's thermodynamics. One zinc ion or two copper ions are bound in Apo-HCA's binds one zinc ion or two copper ions. Our results show that binding at the active site coordinates 6-8 residues; however, copper binding near the N-terminus results in a net unfolding of 6-7 residues. In addition to highlighting a new binding-induced unfolding process, we also show the benefits of calorimetry for investigating metal binding's structural implications.

Source link: https://europepmc.org/article/MED/34989562


Engineered Metal-Binding Sites to Probe Protein Folding Transition States: Psi Analysis.

The formation of the transition state ensemble signifies the first step in protein folding, as shown by the rate-limiting step in protein folding. TSE's structural characteristics remain a challenge. Several causes can obstruct the translation of point mutations in the commonly used technique, "mutational Phi analysis," which could obscure the translation of point mutations. We take a complementary role in "Psi analysis," employing purposefully introduced metal binding sites intended to investigate pairwise contacts in the TSE. The method has been applied to many proteins and consistently produces a much more organized and native-like TSE than Phi analysis.

Source link: https://europepmc.org/article/MED/34845602


Bimetallic Mn, Fe, Co, and Ni Sites in a Four-Helix Bundle Protein: Metal Binding, Structure, and Peroxide Activation.

Small-molecule conversions that are one of the top ten challenges in chemistry are bimetallic active sites in enzymes that catalyze small-molecule reactions. As different metal cofactors are typically embedded in diverse protein scaffolds, it is difficult to decoupage the individual contributions of the metal and the protein matrix to the activity's activity. We compared four homobimetallic cofactors reconstituted into a four-helix bundle protein here, comparing their structure, stability, and hydrogen peroxide reactivity.

Source link: https://europepmc.org/article/MED/34757735


The Small Metal-Binding Protein SmbP Simplifies the Recombinant Expression and Purification of the Antimicrobial Peptide LL-37.

We explore the production of LL-37 tagged with SmbP, a relatively new carrier protein that increases the production of recombinant proteins and peptides in Escherichia coli due to its importance. coli produces a type of recombinant proteins and peptides. Methods: SmbP_LL-37's DNA was converted into E. coli BL21 after overnight expression; after overnight expression, the protein was purified directly from the cell lysate using immobilized metal affinity chromatography, a DNA construct was converted into E. coli BL21; To obtain the free LL-37 peptide, enterokinase was treated with Enterokinase. Using the colony forming unit assay method, the antimicrobial activity of both SmbP_LL-37 and free LL-37 was determined. SmbP_LL-37 was manufactured from one liter of cell culture, yielding a total of 3. 6 grams of SmbP_LL-37. Both SmbP_LL-37 and free LL-37, as well as free LL-37, displayed inhibition against Staphylococcus aureus and Escherichia coli. Conclusions: The SmbP fusion protein is a versatile tool for manufacturing biologically active LL-37 peptide.

Source link: https://europepmc.org/article/MED/34680851

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions