Fig. 5: Molecular dynamics (MD) simulations study of FHI and HI.
From: Synthesis of a highly thermostable insulin by phenylalanine conjugation at B29 Lysine
a Structure of FHI, where B29 Lys(Phe)…A19Tyr, B29 Lys(Phe)…A3Val interactions are shown. Atom color code: H (white), C (gray), O (red), and N (blue). Residues A1 to A21 are assigned residue serial numbers from 1 to 21, and residues B1 to B30 are given residue serial numbers from 22 to 51. Some of the residue serial numbers are indicated (gray); b Difference in the population of contact maps of residues in FHI and HI (ΔC = CFHI – CHI). Population, C, of a contact in the contact map is graded from 1.0 (high) to 0.0 (low). High positive (negative) values of ΔC correspond to an increase (decrease) in the population of any contact upon conjugation of phenylalanine in B29 Lys residue. c The probability distributions of the distance between the backbone carbonyl oxygen of B29 Lys/B29 Lys(Phe) and backbone amide hydrogen of A3Val, and the distance between the center of mass of aromatic rings of B29 Lys(Phe) and A19Tyr. d Root mean square fluctuations (RMSFs) of residues of FHI as compared to that of HI.
