Structural Studies on Inteins
Year: 2013
Type: dissertation
Abstract: Inteins are proteins that have an unusual function. Intein are intervening protein sequences that catalysis there own excitation from a protein precursor sequence. Simultaneously, the intein coordinate the ligation of the flanking sequences. This reaction is called protein splicing. The role of inteins is unclear because they do not provide any benefit or disadvantage to the host organism but inteins has been found to have numerous biotechnological applications. In this thesis NMR spectroscopy and X-ray crystallography have been used to determine the 3D-structures inteins. The combination of the two different techniques has provided important insight about intein mechanism and how inteins could be engineered for application purposes. Proteins are dynamic molecules and NMR spectroscopy was used to indentify flexible sites of studied inteins. The study provided basics insight how to engineer intein for biotechnological application like site-specific modifications. High-resolution crystal structure provided novel insight in possible mechanism of inteins. The data suggest there exist an open and closed form of inteins where the closed conformation has been described in this work. The closed conformation is one of several possible conformations the intein experience while performing the reaction. The structure-functional relationship of inteins is not well understood but this thesis has gain further understanding of the structure aspect of inteins. The work provides further knowledge and guide how inteins can be optimized for possible biotechnological applications.
Source: Työväentutkimus Vuosikirja
Author: Jesper S Øemig
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2118298777