Biomedical Engineering Reference
In-Depth Information
(7) of C chain of collagen also forms one hydrogen bond through Nitrogen with bond
distance of 2.88 and 2.68.
table 3.
Interaction sites, binding energy, hydrogen bond sites and bond distance, calculated based
on the bioinformatics tools for the cross-linking between collagen (Type III) and alginic acid.
Interaction site
Binding energy
(kcal/mol)
H-bond
Bond distance
(Å)
Eleventh residue Ala of A-chain
(α
1
)
-7.14
3.29,3.04,2.85
Ala A 11-(C
α
)-N
H-O(AA)
Ninth residue Ala of C-chain (α
1
)
Ala C 9-(C
α
)-N
H-O(AA)
2.78,3.54
Seventh residue Gly of C-chain
(α
1
)
Gly C 7-(C
α
)-O
H-O(AA)
2.88,2.68
Seventh residue Gly of C-chain
(α
1
)
-6.89
Gly C 7-(C
α
)-O
H-O(AA)
3.27
Eleventh residue Ala of A-chain
(α
1
)
Ala A 11-(C
α
)-N
H-O(AA)
3.02,2.97,3.03
Eleventh residue Ala of A-chain
(α
1
)
-6.5
Ala A 11-(C
α
)-N
H-O(AA)
3.08,2.98
Ninth residue Ala of C-chain (α
1
)
Ala C 9-(C
α
)-N
H-O(AA)
2.78
Seventh residue Gly of C-chain
(α
1
)
Gly C 7-(C
α
)-O
H-O(AA)
2.57
Twelfth residue Lys of A-chain
(α
1
)
-6.07
Lys A 12-(C
α
)-N
H-O(AA)
2.88,3.10
Thirteenth residue Gly of A-chain
(α
1
)
Gly A 13-(C
α
)-O
H-O(AA)
2.89,3.12
Thirteenth residue Gly of A-chain
(α
1
)
-5.92
Gly A 13-(C
α
)-O
H-O(AA)
3.22,2.79,2.59
Fourteen residue Pro of A-chain
(α
1
)
Pro A 14-(C
α
)-N
H-O(AA)
3.53
Twelfth residue Lys of A-chain
(α
1
)
Lys A 12-(C
α
)-N
H-O(AA)
3.25,3.32
Figure 5.
(a) and (b).
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