Sentence examples for membrane protein evolution from inspiring English sources
That study and our study together demonstrate the importance of rigorous statistical analysis in studying membrane protein evolution.
Three recent studies (Kauko et al. 2008; Oberai et al. 2009; Illergard et al. 2010) pioneered the use of a continuous measure of solvent exposure for studying membrane protein evolution.
It was shown that the slower evolutionary rate of TM regions of mammalian GPCRs cannot be entirely explained by their higher average RSA, and thus the membrane environment must play an additional role in shaping membrane protein evolution.
In addition to the new structure-based interpretation of existing sequence conservation and mutational data the models enable, they illustrate the complex transformations occurring in membrane protein evolution: for example, the changes in YeiH and RarD structural element connectivity compared to previously known structures.
Apart from the shared GAIN domain, PKD proteins are unrelated to cell-adhesion GPCRs but also undergo autoproteolysis (Ponting et al, 1999), indicating that the GAIN domain has been utilized by at least two different membrane protein families during evolution.
Thus it was suggested that the ancient intron insertion sites, which are intrinsically related to the functionally key region of the proteins, in the eukaryotic genome, or possibly in the prokaryotic and eukaryotic common ancestor, and the unique palindromic genomic duplication in the genomes of vertebrate clade shaped an elementally functioning membrane protein family during evolution.
The fact that uroplakins 1a and 1b (UPK1andnd UPK1b) interact specifically with uroplakins 2 and 3a (UPK2 and UPK3a), respectively, make them an attractive system for studying the co-evolution of interacting membrane protein pairs [ 14- 16].
The fundamental difference in biophysical properties between membrane and aqueous environments and its effects on protein evolution are expected to be largely species independent.
β2-m is a small membrane protein (11800 D) that is highly stable during evolution; it is encoded in the sixth chromosome.
The PG-binding domains are believed to have been acquired by MotBs and other OmpA-like proteins from a common ancestor early in evolution, before MotBs and the outer membrane protein family diverged from each other.
TA proteins are conserved throughout evolution [30] and may represent one of the most primitive membrane protein architectures.
