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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Amino Acids. 2012 Oct 30;44(3):821–833. doi: 10.1007/s00726-012-1421-9

Fig. 1.

Fig. 1

(A) Arginine–phosphate and (B) Lysine–phosphate complexes stabilized by N-H⋯O-P H-bonds in POPC-POPG-bound CPP penetratin. The structural models were built based on experimentally measured site-specific 13C-31P distances (solid line) (Su et al, 2011), sidechain dihedral angles from the penultimate rotamer library (Lovell et al, 2000) and N-H⋯O-P geometric parameters in previous studies (Zhang et al, 1999; de Dios and Oldfield, 1994). Geometry parameters of the N-H⋯OP H-bonds: θ =120°, σ =168° and r = 2.8 Å. (C) Guanidinium-phosphate and guanidinium-water interactions of POPE-POPG-bound PG-1.