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Figure 4 | BMC Research Notes

Figure 4

From: Implication of the cause of differences in 3D structures of proteins with high sequence identity based on analyses of amino acid sequences and 3D structures

Figure 4

Visuallization of hydrophobic packings. (a) The packing hydrophobic residues formed by residues near the peaks of the F-value plot for 2LHC (GA98-1). The packing residues are 16-A, 20-L, 30-F, 33-I, 42-V and 45-L. (b) The hydrophobic contacts formed by residues near the peaks of the F-value plot for 2LHD (GB98-1). The pairwise contacts are formed by 16-Ala and 30-Phe, 20-Leu and 26-Ala as well as by 34-Ala and 43-Trp. 35-Asn, which forms a contact with 43-Trp in Gō model simulations, is indicated by light gray. (c) The packing hydrophobic residues formed by residues near the peaks of the F-value plot for 2LHG (GA98-2). The packing residues are 16-A, 20-L,25-I, 33-I, 42-V and 45YL. (d) The hydrophobic contacts formed by residues near the peaks of the F-value plot for 2LHE (GB98-2). The pairwise contacts are formed by 16-Ala and 30-Phe, 20-Leu and 25-Ile as well as by 34-Ala and 43-Trp.

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