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Application of molecular dynamics simulations to design a dual-purpose oligopeptide linker sequence for fusion proteins |
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| Authors: | Ehsan?Rezaie,Mozafar?Mohammadi author-information" > author-information__contact u-icon-before" > mailto:mohammadi@live.com" title=" mohammadi@live.com" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author,Amirhossein?Sakhteman,Peyman?Bemani,Sajjad?Ahrari |
| Affiliation: | 1.Applied Biotechnology Research Center,Baqiyatallah University of Medical Sciences,Tehran,Iran;2.Department of Biology, Faculty of Science,Razi University,Kermanshah,Iran;3.School of Pharmacy,Shiraz University of Medical Sciences,Shiraz,Iran;4.Department of Immunology,Shiraz University of Medical Sciences,Shiraz,Iran;5.Department of Pharmaceutical Biotechnology, Pharmaceutical Science Research Center, Faculty of Pharmacy,Shiraz University of Medical Sciences,Shiraz,Iran |
| Abstract: | Proteins are often monitored by combining a fluorescent polypeptide tag with the target protein. However, due to the high molecular weight and immunogenicity of such tags, they are not suitable choices for combining with fusion proteins such as immunotoxins. In this study, we designed a polypeptide sequence with a dual role (it acts as both a linker and a fluorescent probe) to use with fusion proteins. Two common fluorescent tag sequences based on tetracysteine were compared to a commonly used rigid linker as well as our proposed dual-purpose sequence. Computational investigations showed that the dual-purpose sequence was structurally stable and may be a good choice to use as both a linker and a fluorescence marker between two moieties in a fusion protein. |
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