BOHM, G and JAENICKE, R (1994) RELEVANCE OF SEQUENCE STATISTICS FOR THE PROPERTIES OF EXTREMOPHILIC PROTEINS. INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH, 43 (1). pp. 97-106. ISSN 0367-8377,
Full text not available from this repository.Abstract
The amino acid composition of proteins from mesophilic and extremophilic organisms is commonly assumed to reflect the mechanisms of molecular adaptation to extremes of physical conditions. In this context, halophilic behaviour has been attributed to significantly increased numbers of aspartic and glutamic acid residues. However, extending the analysis to a statistically relevant set of related proteins, dihydrofolate reductase from Halobacterium vokanii, as an example, shows that the increase in negative charge is found to be less significant than other exchanges of amino acids (e.g., Ala, Asn, Arg, Lys, Phe, Ser). Thus, the high water binding capacity of negatively charged residues cannot be unambiguously correlated with the anomalous stability of halophilic proteins. A similar caveat holds for generalizations regarding the thermal stability of proteins. In this case, D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima was compared with a number of mesophilic and moderately thermophilic homologs. Again, 'traffic rules of stabilization', in terms of amino acid changes in going from mesophilic to thermophilic proteins, cannot be given. (C) Munksgaard 1994.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DIHYDROFOLATE-REDUCTASE GENE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE GENE; AMINO-ACID-SEQUENCE; NUCLEOTIDE-SEQUENCE; ESCHERICHIA-COLI; METHANOTHERMUS-FERVIDUS; THYMIDYLATE SYNTHASE; GENOMIC ORGANIZATION; HALOPHILIC PROTEINS; THERMAL-STABILITY; EXTREMOPHILIC PROTEINS; HALOPHILY; MOLECULAR MODELING; SEQUENCE STATISTICS; THERMOPHILY |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53550 |
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