AMINO ACIDS SEQUENCE ANALYSIS ON COLLAGEN



between Bos taurus - Canis lupus, Homo sapiens - Bos Taurus, Bos taurus - Danio rerio, and
Canis lupus - Danio rerio; ■ a good similarity on α2 chain exists between Bos taurus - Canis
lupus
, Homo sapiens - Canis lupus, and Homo sapiens - Bos taurus.

Table 3.

Collagen chains similarity matrix (expressed as percent)

BT α1

BT α2

CL α1

CL α2

DR α1

DR α2

HS α1

HS α2

RN α1

BT_a1 = Bos taurus CTIα1

100

BT_a2 = Bos taurus CTIα2

47.19

100

CL_a1 = Canis lupus CTIα1

97.43

47.38

100

CL_a2 = Canis lupus CTIα2

48.71

94.51

50.18

100

DR_a1 = Danio rerio CTIα1

75.74

49.38

76.37

47.00

100

DR_a2 = Danio rerio CTIα2

42.77

60.16

43.46

58.13

36.73

100

HS_a1 = Homo sapiens CTIα1

82.39

35.35

82.56

34.58

62.56

38.08

100

HS_a2 = Homo sapiens CTI α2

53.23

93.33

52.09

94.51

49.41

66.15

40.49

100

RN_a1 = Rattus norvegicus CTIα1

72.79

20.93

72.32

20.58

44.22

22.11

74.05

9.34

100

RN_a2= Rattus norvegicus CTI α2

18.64

70.63

14.00

66.56

25.80

40.62

15.18

66.97

38.94

Table 4.

Collagen chains Levenshtein distances within and between species

BT α1

BT α2

CL α1

CL α2

DR α1

DR α2

HS α1

HS α2

RN α1

BT α1

_____0

BT α2

903

~~0

CL α1

____70

892

_____0

CL α2

893

____98

891

_____0

DR α1

469

902

440

896

______0

DR α2

909

463

903

492

909

~~0

HS_a1

429

882

448

883

731

871

_____0

HS α2

884

115

883

____76

895

487

874

_____0

RN α1

1031

921

1033

921

1016

890

650

923

______0

RN α2

1061

941

1059

944

1044

923

671

940

428

The Levenshtein distances, defined as the minimal numbers of characters that must be
replace, insert or delete to transform one chain into other are presented in Table 4. With
seventy amino acids characters replace, insert or delete the α1 collagen type I chain of
Bos
taurus
could be transformed in α1 collagen type I chain of Canis lupus. With ninety-eight
amino acids characters replace, insert or delete the α2 collagen type I chain of
Bos taurus
could be transformed in α2 collagen type I chain of Canis lupus. The greater dissimilarity was
identified when collagen type I chains of
Rattus norvegicus are compared with other species
(see Table 3 and 4). This could be explained by the existence of a great number of unknown
or unidentified amino acids and/or by the absence of the cysteine and tryptophan (see Table
1).

CONCLUSIONS

The scale of amino acids hydrophobic or hydrophilic is still on debate even if there
were proposed many methods. The scale proposed by Welling et al. seems to be more stable
on principal component analysis on investigated scales.

The similarity analysis revealed that there are good similarities on Collagen type I
amino acids chains between
Bos Taurus and Canis lupus, as well as between Bos Taurus and
Homo sapiens. Due to the lack of amino acids identification on collagen type I of Rattus
norvegicus
the greatest dissimilarities were observed when this specie was compared with the
other analyzed species.

314



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