DFT Study on the His-Tag Binding Affinity of Metal Ions in Modeled Hexacationic Metal Complexes
 
Yazarlar (4)
Arş. Gör. Alparslan Numan Yildiz İstanbul Teknik Üniversitesi, Türkiye
Prof. Dr. Emine Esra KASAPBAŞI Haliç Üniversitesi, Türkiye
Zeynep Yurtsever
Enplusone Biosciences Inc., Amerika Birleşik Devletleri
Prof. Dr. Mine Yurtsever İstanbul Teknik Üniversitesi, Türkiye
Makale Türü Açık Erişim Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı ACS Omega (Q2)
Dergi ISSN 2470-1343 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI
Makale Dili Türkçe Basım Tarihi 11-2024
Kabul Tarihi Yayınlanma Tarihi 08-11-2024
Cilt / Sayı / Sayfa 9 / 46 / 45920–45925 DOI 10.1021/acsomega.4c05422
Makale Linki https://doi.org/10.1021/acsomega.4c05422
UAK Araştırma Alanları
Fiziksel Kimya
Özet
Histidine oligomers (His-tags) are commonly used as affinity tags in recombinant protein purification to enable in vitro experimental studies, including biochemical and biophysical assays and structure determination. His-tags enable protein purification by specifically and efficiently coordinating bivalent metal ions present in the purification resins, such as Cu2+, Zn2+, and Ni2+. Although His-tags, combined with Ni2+-based resins, are widely used due to their biophysical properties and commercial availability, the structure and nature of the metal cation coordination have remained unclear. In this study, the chemical structure of metal-coordinating His-tags was modeled to elucidate the metal preferences for better binding and to determine the structural changes that occur upon metal coordination. 6His-tag is a string of 6 histidine residues usually coordinated to bivalent metal ions (M2+), such as Ni2+, Zn2+, and Cu2 …
Anahtar Kelimeler
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
Web of Science 7
Scopus 7
Google Scholar 6
DFT Study on the His-Tag Binding Affinity of Metal Ions in Modeled Hexacationic Metal Complexes

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