Polymer mediated protein crystallisation
Structure elucidation of a macromolecule can lead to the determination of its function. In the case of proteins, knowledge of their three-dimensional structure can be utilised in the identification of active site(s) and consequently in rational drug design. Commonly, X-ray crystallography is imple...
| Main Author: | |
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| Format: | Thesis (University of Nottingham only) |
| Language: | English |
| Published: |
2013
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| Online Access: | https://eprints.nottingham.ac.uk/13192/ |
| _version_ | 1848791674070761472 |
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| author | Nikolaidi, Dimitra |
| author_facet | Nikolaidi, Dimitra |
| author_sort | Nikolaidi, Dimitra |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | Structure elucidation of a macromolecule can lead to the determination of its function. In the case of proteins, knowledge of their three-dimensional structure can be utilised in the identification of active site(s) and consequently in rational drug design. Commonly, X-ray crystallography is implemented on a high quality single crystal of the target macromolecule, in order to elucidate its structure. Moreover, crystallised protein molecules may remain active which can then be used in controlled drug delivery. Unfortunately, the successful crystallisation of a macromolecule can be seen as the most challenging aspect in this endeavour, given that predicting, screening and directing crystallisation remains an elusive goal.
A possible solution to this problem is the use of heterogeneous nucleation, where a foreign surface is employed to lower the energy barrier for nucleation to occur. Heteronucleation has been utilised in the crystallisation of small organic molecules, inorganic complexes, extended networks and proteins. Polymeric surfaces, as heteronucleants, in protein crystallisation have been known to increase nucleation density rates and selectively crystallise particular forms of proteins. Moreover, imprinted polymeric surfaces have been successfully used to selectively crystallise inorganic molecules as well as a small range of well studied proteins.
This thesis presents the effects of polymers on the crystallisation of two proteins, that of mutant human thioredoxin and wild-type hen egg-white lysozyme (HEWL). Polymers were used in solution, as physically adsorbed films as well as plasma polymers. Shape and size of the protein crystals was altered, while polymorphism was also achieved, in the presence of polymers with various functionalities. This work is a step towards the use of polymers as heteronucleants in directing protein crystallisation. |
| first_indexed | 2025-11-14T18:32:15Z |
| format | Thesis (University of Nottingham only) |
| id | nottingham-13192 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T18:32:15Z |
| publishDate | 2013 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-131922025-02-28T11:23:42Z https://eprints.nottingham.ac.uk/13192/ Polymer mediated protein crystallisation Nikolaidi, Dimitra Structure elucidation of a macromolecule can lead to the determination of its function. In the case of proteins, knowledge of their three-dimensional structure can be utilised in the identification of active site(s) and consequently in rational drug design. Commonly, X-ray crystallography is implemented on a high quality single crystal of the target macromolecule, in order to elucidate its structure. Moreover, crystallised protein molecules may remain active which can then be used in controlled drug delivery. Unfortunately, the successful crystallisation of a macromolecule can be seen as the most challenging aspect in this endeavour, given that predicting, screening and directing crystallisation remains an elusive goal. A possible solution to this problem is the use of heterogeneous nucleation, where a foreign surface is employed to lower the energy barrier for nucleation to occur. Heteronucleation has been utilised in the crystallisation of small organic molecules, inorganic complexes, extended networks and proteins. Polymeric surfaces, as heteronucleants, in protein crystallisation have been known to increase nucleation density rates and selectively crystallise particular forms of proteins. Moreover, imprinted polymeric surfaces have been successfully used to selectively crystallise inorganic molecules as well as a small range of well studied proteins. This thesis presents the effects of polymers on the crystallisation of two proteins, that of mutant human thioredoxin and wild-type hen egg-white lysozyme (HEWL). Polymers were used in solution, as physically adsorbed films as well as plasma polymers. Shape and size of the protein crystals was altered, while polymorphism was also achieved, in the presence of polymers with various functionalities. This work is a step towards the use of polymers as heteronucleants in directing protein crystallisation. 2013-07-10 Thesis (University of Nottingham only) NonPeerReviewed application/pdf en arr https://eprints.nottingham.ac.uk/13192/1/Dimitra%27s_Thesis_-_Final.pdf Nikolaidi, Dimitra (2013) Polymer mediated protein crystallisation. MPhil thesis, University of Nottingham. |
| spellingShingle | Nikolaidi, Dimitra Polymer mediated protein crystallisation |
| title | Polymer mediated protein crystallisation |
| title_full | Polymer mediated protein crystallisation |
| title_fullStr | Polymer mediated protein crystallisation |
| title_full_unstemmed | Polymer mediated protein crystallisation |
| title_short | Polymer mediated protein crystallisation |
| title_sort | polymer mediated protein crystallisation |
| url | https://eprints.nottingham.ac.uk/13192/ |