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dc.contributor.authorKahlke, Tim
dc.contributor.authorThorvaldsen, Steinar
dc.date.accessioned2013-03-08T07:26:54Z
dc.date.available2013-03-08T07:26:54Z
dc.date.issued2012
dc.description.abstractCold-adaptation strategies have been studied in multiple psychrophilic organisms, especially for psychrophilic enzymes. Decreased enzyme activity caused by low temperatures as well as a higher viscosity of the aqueous environment require certain adaptations to the metabolic machinery of the cell. In addition to this, low temperature has deleterious effects on the lipid bilayer of bacterial membranes and therefore might also affect the embedded membrane proteins. Little is known about the adaptation of membrane proteins to stresses of the cold. In this study we investigate a set of 66 membrane proteins from the core genome of the bacterial family Vibrionaceae to identify general characteristics that discern psychrophilic and mesophilic membrane proteins. Bioinformatical and statistical methods were used to analyze the alignments of the three temperature groups mesophilic, intermediate and psychrophilic. Surprisingly, our results show little or no adaptation to low temperature for those parts of the proteins that are predicted to be inside the membrane. However, changes in amino acid composition and hydrophobicity are found for complete sequences and sequence parts outside the lipid bilayer. Among others, the results presented here indicate a preference for helix-breaking and destabilizing amino acids Ile, Asp and Thr and an avoidance of the helix-forming amino acid Ala in the amino acid composition of psychrophilic membrane proteins. Furthermore, we identified a lower overall hydrophobicity of psychrophilic membrane proteins in comparison to their mesophilic homologs. These results support the stability-flexibility hypothesis and link the cold-adaptation strategies of membrane proteins to those of loop regions of psychrophilic enzymes.en
dc.descriptionThis article is part of Tim Kalkhe's doctoral thesis, available in Munin at <a href=http://hdl.handle.net/10037/5248>http://hdl.handle.net/10037/5248</a>
dc.identifier.citationPLoS ONE (2012), vol. 7(12): e51761en
dc.identifier.cristinIDFRIDAID 976255
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0051761
dc.identifier.issn1932-6203
dc.identifier.urihttps://hdl.handle.net/10037/4922
dc.identifier.urnURN:NBN:no-uit_munin_4629
dc.language.isoengen
dc.publisherPublic Library of Science (PLoS)en
dc.rights.accessRightsopenAccess
dc.subjectVDP::Mathematics and natural science: 400::Basic biosciences: 470::Molecular biology: 473en
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Basale biofag: 470::Molekylærbiologi: 473en
dc.titleMolecular Characterization of Cold Adaptation of Membrane Proteins in the Vibrionaceae Core-Genomeen
dc.typeJournal articleen
dc.typeTidsskriftartikkelen
dc.typePeer revieweden


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