- Title
- Analysis of protein thermostability enhancing factors in industrially important thermus bacteria species
- Creator
- Kumwenda, Benjamin, Litthauer, Derek, Tastan Bishop, Özlem, Reva, Oleg
- Date
- 2013
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/123085
- Identifier
- vital:35404
- Identifier
- https://doi.10.4137/EBO.S12539
- Description
- Elucidation of evolutionary factors that enhance protein thermostability is a critical problem and was the focus of this work on Thermus species. Pairs of orthologous sequences of T. scotoductus SA-01 and T. thermophilus HB27, with the largest negative minimum folding energy (MFE) as predicted by the UNAFold algorithm, were statistically analyzed. Favored substitutions of amino acids residues and their properties were determined. Substitutions were analyzed in modeled protein structures to determine their locations and contribution to energy differences using PyMOL and FoldX programs respectively. Dominant trends in amino acid substitutions consistent with differences in thermostability between orthologous sequences were observed. T. thermophilus thermophilic proteins showed an increase in non-polar, tiny, and charged amino acids. An abundance of alanine substituted by serine and threonine, as well as arginine substituted by glutamine and lysine was observed in T. thermophilus HB27. Structural comparison showed that stabilizing mutations occurred on surfaces and loops in protein structures.
- Format
- 16pages, pdf
- Language
- English
- Relation
- Evolutionary Bioinformatics, Kumwenda, B., Litthauer, D., Bishop, Ö.T. and Reva, O., 2013. Analysis of protein thermostability enhancing factors in industrially important thermus bacteria species. Evolutionary Bioinformatics, 9, pp.EBO-S12539, Evolutionary Bioinformatics volume 9 number 327 342 2013 1176-9343
- Rights
- Evolutionary Bioinformatics
- Rights
- Use of this resource is governed by the terms and conditions of the Sage Journals Terms of Use statement (https://journals.sagepub.com/page/policies/terms-of-use)
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Tastan Bishop, Ozlem (Prof)
RU Research Unit in Bioinformatics (RUBi)
RU Department of Biochemistry, Microbiology and Bioinformatics
SDG 03. Good Health and Well-Being
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| View Details | SOURCE1 | Analysis of Protein Thermostability Enhancing Factors.pdf | 1 MB | Adobe Acrobat PDF | View Details |