APPLICATION OF 3-DIMENSIONAL MOLECULAR HYDROPHOBICITY POTENTIAL TO THE ANALYSIS OF SPATIAL-ORGANIZATION OF MEMBRANE-PROTEIN DOMAINS .2. OPTIMIZATION OF HYDROPHOBIC CONTACTS IN TRANSMEMBRANE HAIRPIN STRUCTURES OF NA+, K+-ATPASE

A method of packing of transmembrane hairpin helices in proteins is described. The procedure is based on the optimization of hydrophobic contacts calculated using the three-dimensional (3D) molecular hydrophobicity potential technique. To verify the validity of the computational scheme, we calculated relative orientations of membrane-spanning peptides in pairs L2-L3, M2-M3, and M4-M5 from L- and M-subunits of the photoreaction center of Rhodopseudomonas viridis and compared the predicted structures with those derived from atomic coordinates. The results of computer modeling agree with the X-ray data. We applied the approach proposed to study possible interhelical interactions in transmembrane hairpin structures of Na+, K+-ATPase.