Mutation at a Single Acidic Amino Acid Enhances the Halophilic Behaviour of Malate Dehydrogenase from Haloarcula Marismortui in Physiological Salts
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.tb20659.x/fullpdf
Reference48 articles.
1. Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui.
2. Functional implications related to the gene structure of the elongation factor EF-Tu fromHalobacterium marismortui
3. The gene for a halophilic glutamate dehydrogenase sequence, transcription analysis and phylogenetic implications
4. PCR-mediated cloning and sequencing of the gene encoding glutamate dehydrogenase from the archaeon Sulfolobus shibatae: identification of putative amino-acid signatures for extremophilic adaptation
5. Relevance of sequence statistics for the properties of extremophilic proteins
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