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Table 3 Pairwise parameters for candidate alkane hydroxylases in two conserved pfam domains, p450 and Pry_redox_3

From: Alkane hydroxylase genes in psychrophile genomes and the potential for cold active catalysis

pfam domain Protein region Protein parameter Total number of comparisons1 Cases where psychrophile was higher
p450 Whole Isoelectric point 9 0
p450 Whole Asparagine 9 8
p450 Whole Arginine 9 0
p450 Whole Threonine 9 8
p450 Whole Valine 9 9
p450 Coil Isoleucine 9 8
p450 Coil Aspargine 9 9
p450 Coil Valine 9 9
p450 β-sheet Flexibility 9 8
p450 β-sheet Isoelectric point 9 8
p450 β-sheet Alanine 9 8
p450 β-sheet Glycine 9 9
p450 β-sheet Isoleucine 9 1
p450 β-sheet Proline 9 9
p450 α-helix Flexibility 9 8
p450 α-helix Aspartic acid 9 9
p450 α-helix Isoleucine 9 0
p450 α-helix Arginine 9 0
Pyr_redox_3 Whole Cysteine 11 10
Pyr_redox_3 Whole Glutamic acid 11 0
Pyr_redox_3 Whole Valine 11 10
Pyr_redox_3 Coil Aspartic acid 11 10
Pyr_redox_3 Coil Glycine 11 1
Pyr_redox_3 β-sheet GRAVY 11 10
Pyr_redox_3 β-sheet Cysteine 11 11
Pyr_redox_3 α-helix Alanine 11 10
Pyr_redox_3 α-helix Glutamic acid 11 0
Pyr_redox_3 α-helix Asparagine 11 1
  1. Amino acids in the parameter column refer to amino acid content.
  2. 1All psychrophile candidate alkane hydroxylases within a pfam were compared with all mesophile candidate alkane hydroxylases in that pfam for a given protein secondary structure (region), protein parameter, and taxonomic pair, where the total number of comparisons possible was 9 or 11 (see Table 2).