Photoactivatable Inteins and Nanobodies: New Tools for Protein Control Inteins remove themselves out of a precursor protein in a process termed protein splicing. The flanking sequences, termed exteins, are ligated to give the mature host protein. Furthermore, in protein trans-splicing, the intein domain is split into two fragments and the extein sequences are ligated from two separate precursor proteins. The unique structural changes associated with protein splicing and protein transsplicing have inspired the development of many protein tools ranging from protein purification, protein biotechnology and protein chemical modification to synthetic biology. We have identified several new split inteins and further customized them by protein engineering approaches, in particular for applications in protein chemical modification[1] and light-control of protein splicing[2] (Figure 1). In this talk, I will underline the rationales behind the design of photoactivatable inteins and discuss potential applications. On a similar note, we rendered nanobodies (single-domain antibody fragments) photoactivatable to have light control over their antigen binding.[3] Design and applications of the so-called photobodies will be briefly presented. Host: Dr Baojun Wang The Mootz Lab is interested in how proteins work on the molecular level. For this purpose, they develop novel approaches for the site-specific chemical modification of proteins and for the experimental control of their activity by external stimuli like small ligands or light. Ultimately, their research is also geared towards applying these techniques to study proteins in their natural environment, the living cell. Their methodology combines expertises at the interface of chemistry and biology. Jun 17 2021 12.00 - 13.00 Photoactivatable Inteins and Nanobodies: New Tools for Protein Control Seminar by Prof. Henning Mootz (Institute of Biochemistry, University of Münster) Online via Zoom Contact j.fyffe@ed.ac.uk
Photoactivatable Inteins and Nanobodies: New Tools for Protein Control Inteins remove themselves out of a precursor protein in a process termed protein splicing. The flanking sequences, termed exteins, are ligated to give the mature host protein. Furthermore, in protein trans-splicing, the intein domain is split into two fragments and the extein sequences are ligated from two separate precursor proteins. The unique structural changes associated with protein splicing and protein transsplicing have inspired the development of many protein tools ranging from protein purification, protein biotechnology and protein chemical modification to synthetic biology. We have identified several new split inteins and further customized them by protein engineering approaches, in particular for applications in protein chemical modification[1] and light-control of protein splicing[2] (Figure 1). In this talk, I will underline the rationales behind the design of photoactivatable inteins and discuss potential applications. On a similar note, we rendered nanobodies (single-domain antibody fragments) photoactivatable to have light control over their antigen binding.[3] Design and applications of the so-called photobodies will be briefly presented. Host: Dr Baojun Wang The Mootz Lab is interested in how proteins work on the molecular level. For this purpose, they develop novel approaches for the site-specific chemical modification of proteins and for the experimental control of their activity by external stimuli like small ligands or light. Ultimately, their research is also geared towards applying these techniques to study proteins in their natural environment, the living cell. Their methodology combines expertises at the interface of chemistry and biology. Jun 17 2021 12.00 - 13.00 Photoactivatable Inteins and Nanobodies: New Tools for Protein Control Seminar by Prof. Henning Mootz (Institute of Biochemistry, University of Münster) Online via Zoom Contact j.fyffe@ed.ac.uk
Jun 17 2021 12.00 - 13.00 Photoactivatable Inteins and Nanobodies: New Tools for Protein Control Seminar by Prof. Henning Mootz (Institute of Biochemistry, University of Münster)
