Editing Halophile (section)

== Genomic and proteomic signature ==

The comparative genomic and proteomic analysis showed distinct molecular signatures exist for the environmental adaptation of halophiles. At the protein level, the halophilic species are characterized by low hydrophobicity, an overrepresentation of acidic residues, underrepresentation of Cys, lower propensities for helix formation, and higher propensities for coil structure. The core of these proteins is less hydrophobic, such as [[DHFR]], that was found to have narrower β-strands.<ref>{{cite journal | vauthors = Kastritis PL, Papandreou NC, Hamodrakas SJ | date = October 2007 | title = Haloadaptation: Insights from comparative modeling studies of halophilic archaeal DHFRs | journal = International Journal of Biological Macromolecules | volume = 41 | issue = 4 | pages = 447–453 | pmid = 17675150 | doi = 10.1016/j.ijbiomac.2007.06.005 }}</ref>
In one study, the net charges (at pH 7.4) of the ribosomal proteins (r-proteins) that comprise the ''S10-spc'' cluster were observed to have an inverse relationship with the halophilicity/halotolerance levels in both bacteria and archaea.<ref>{{cite journal | vauthors = Tirumalai MR, Anane-Bediakoh D, Rajesh S, Fox GE| date = December 2021 | title = Net Charges of the Ribosomal Proteins of the S10 and spc Clusters of Halophiles Are Inversely Related to the Degree of Halotolerance | journal = Microbiol Spectr| volume = 9 | issue = 3 | page = e0178221 | pmid = 34908470 | pmc = 8672879 | doi = 10.1128/spectrum.01782-21 }}</ref> At the DNA level, the halophiles exhibit distinct dinucleotide and codon usage.<ref>{{cite journal | vauthors = Paul S, Bag SK, Das S, Harvill ET, Dutta C | date = April 2008 | title = Molecular signature of hypersaline adaptation: insights from genome and proteome composition of halophilic prokaryotes | journal = Genome Biology | volume = 9 | issue = 4 | page = R70 | pmid = 18397532 | pmc = 2643941 | doi = 10.1186/gb-2008-9-4-r70 | doi-access = free }}</ref>