ArticleInorganic chemistry2022
Metal Ion Binding Induces Local Protein Unfolding and Destabilizes Human Carbonic Anhydrase II.
Article in Inorganic chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 13 citations in OpenAlex.
- Platinum Stabilises a Molten-Globule Conformation of a Small Globular Cytosolic Protein SUMO1.Chemistry, an Asian journal · 2025Article
- Comparative Toxicity of Interferon Beta-1a Impurities of Heavy Metal Ions.Medicina (Kaunas, Lithuania) · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Human carbonic anhydrase II (HCA) is a robust metalloprotein and an excellent biological model system to study the thermodynamics of metal ion coordination. Apo-HCA binds one zinc ion or two copper ions. We studied these binding processes at five temperatures (15-35 °C) using isothermal titration calorimetry, yielding thermodynamic parameters corrected for pH and buffer effects. We then sought to identify binding-induced structural changes. Our data suggest that binding at the active site organizes 6-8 residues; however, copper binding near the N-terminus results in a net
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