Investigation of mutations (L41F, F17M, N57E, Y99F_Y134W) effects on the TolAIII-UnaG fluorescence protein's unconjugated bilirubin (UC-BR) binding ability and thermal stability properties
Yazarlar (4)
Dr. Öğr. Üyesi Numan ECZACIOĞLU Karamanoğlu Mehmetbey Üniversitesi, Türkiye
Prof. Dr. Yakup Ulusu Karamanoğlu Mehmetbey Üniversitesi, Türkiye
Prof. Dr. İsa GÖKÇE Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Jeremy H. Lakey
University of Newcastle Upon Tyne, Faculty of Medical Sciences, İngiltere
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Preparative Biochemistry and Biotechnology (Q3)
Dergi ISSN 1082-6068 Dergi Bilgileri (2022)
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 04-2022
Cilt / Sayı / Sayfa 52 / 4 / 365–374 DOI 10.1080/10826068.2021.1952597
Makale Linki http://dx.doi.org/10.1080/10826068.2021.1952597
UAK Araştırma Alanları
Protein Mühendisliği
Özet
The UnaG protein is a ligand (unconjugated bilirubin) dependent fluorescence protein isolated from Unagi freshwater eel larvae and expressed as fusion in heterologous expression systems. Bilirubin is a tetrapyrrole molecule mainly produced from heme catabolism by the destruction of erythrocytes in the body. Bilirubin can cause kernicterus, a serious condition associated with permanent neurological damage in neonates with the passage of brain tissue. Different methods have been developed for plasma bilirubin analysis and quantification. The use of UnaG fluorescence protein triggered by bilirubin has become a new approach in bilirubin studies. In this study, we aimed to investigate the biophysical characterization of ligand interactions with the proteins obtained as a result of mutations (UnaGY99F_Y134W, UnaGN57E, UnaGL41F, and UnaGF17M) on the amino acid sequence of TolAIII-UnaG protein. After the ...
Anahtar Kelimeler
Bilirubin | fluorescence protein | UnaG