For instance, large subunit group 1 proteins (leaf isoforms) had more conserved sites in the N-terminus while group 3a proteins (sink isoforms) exhibited more conserved in the C-terminus.
Positions of functional and/or structural importance generally tend to be more conserved in a given protein family and therefore to have high conservation indices.
Typically, protein spatial structures are more conserved in evolution than amino acid sequences.
This approach is based on the observation that protein structures are significantly more conserved in evolution than linear sequences, and mechanistic similarities among diverse transporters are emerging.
We observed a similar situation, although, it seems that the C-values are notably more conserved in the floral organs of T. pratense in comparison with the previous studies.
Moreover, tertiary structures tend to be more conserved in evolution and retain the functional properties than sequences [60], [61].
B. garinii variants isolated from patients with LB in southern Sweden were more conserved in their IGS sequence than the variants associated with I. ricinus or I. uriae.
We can see that Group 2 is more conserved in glutamate binding region than Group 1 but less conserved in channel region.
Between the TSA-treated and untreated cells of A. fumigatus, the nucleosome positions were more conserved in the gene promoters than in the gene bodies (Fig. 4).
The orthologs that are involved in CCNs have been shown to be more conserved in gene expression between species [27], which should be a better reference set for cross-species comparison of gene expression than WOS.
It was shown that residues which form many coevolutionary connections with other residues are more conserved in evolution and are involved in functionally important interactions or conformational changes [17], [23], [24].
