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. Author manuscript; available in PMC: 2009 Sep 6.

Published in final edited form as: J Mol Biol. 2007 Dec 4;376(3):736–748. doi: 10.1016/j.jmb.2007.11.075

(a) Diagram showing the nature of residues within all 91 G1G interruptions found in non-fibrillar collagens, where Hydrophobic () = F,I,L,M,V,Y; Charged () = D,E,H,K,R; Polar () = Q,N,T; Small () = A,C,G,S; Pro ().

(b) Histogram showing the observed (gray) versus expected frequencies in X1 position (white) and X2 position (black) of groups of amino acids in G1G interruptions in all non-fibrillar collagens. The expected frequencies were calculated based on the identity of amino acids in the X1 and X2 positions of (Gly-X1-X2)_n sequences of all 6 chains of type IV collagen. A chi square analysis indicates the observed distribution is very different from that expected for the X1 position (p<0.001) and the X2 position (p<0.001), and the major chi square terms come from the high number of hydrophobic residues and lower than expected number of imino acids.

(a) Diagram showing the nature of residues within all 91 G1G interruptions found in non-fibrillar collagens, where Hydrophobic () = F,I,L,M,V,Y; Charged () = D,E,H,K,R; Polar () = Q,N,T; Small () = A,C,G,S; Pro ().

(b) Histogram showing the observed (gray) versus expected frequencies in X1 position (white) and X2 position (black) of groups of amino acids in G1G interruptions in all non-fibrillar collagens. The expected frequencies were calculated based on the identity of amino acids in the X1 and X2 positions of (Gly-X1-X2)_n sequences of all 6 chains of type IV collagen. A chi square analysis indicates the observed distribution is very different from that expected for the X1 position (p<0.001) and the X2 position (p<0.001), and the major chi square terms come from the high number of hydrophobic residues and lower than expected number of imino acids.