Figure 4From: Implication of the cause of differences in 3D structures of proteins with high sequence identity based on analyses of amino acid sequences and 3D structuresVisuallization 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.Back to article page