ArticleFrontiers in molecular biosciences2026
Biophysical insights into recombinant Zeocin binding protein: conformational stability and folding dynamics across pH and temperature.
Article in Frontiers in molecular biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Zeocin-binding protein (ZBP) confers resistance to the bleomycin family of antibiotics across a wide variety of prokaryotic and eukaryotic hosts. Zeocin is a bleomycin derivative used in cancer treatment. ZBP's mechanism involves binding to Zeocin, shielding DNA from damage. In protein folding studies, ZBP, a versatile marker across various organisms, can be used to track protein folding by fusing it to target proteins in prokaryotes and eukaryotes. Despite its significance, ZBP's biophysical properties are poorly studied. This study characterized the conformational changes, pH stability, solubility, and thermodynamic stability of recombinant ZBP from
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