title: Application of three-dimensional molecular hydrophobicity potential to the analysis of spatial organization of membrane domains in proteins: I. Hydrophobic properties of transmembrane segments of Na+, K(+)-ATPase.
abstract: A new computer-aided molecular modeling approach based on the concept of three-dimensional (3D) molecular hydrophobicity potential has been developed to calculate the spatial organization of intramembrane domains in proteins. The method has been tested by calculating the arrangement of membrane-spanning segments in the photoreaction center of Rhodopseudomonas viridis and comparing the results obtained with those derived from the X-ray data. We have applied this computational procedure to the analysis of interhelical packing in membrane moiety of Na+, K(+)-ATPase. The work consists of three parts. In Part I, 3D distributions of electrostatic and molecular hydrophobicity potentials on the surfaces of transmembrane helical peptides were computed and visualized. The hydrophobic and electrostatic properties of helices are discussed from the point of view of their possible arrangement within the protein molecule. Interlocation of helical segments connected with short extramembrane loops found by means of optimization of their hydrophobic/hydrophilic contacts is considered in Part II. The most probable 3D model of packing of helical peptides in the membrane domain of Na+, K(+)-ATPase is discussed in the final part of the work.
authors.affiliation: Shemyakin Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
authors.forename: R G
authors.initials: RG
authors.lastname: Efremov
authors.forename: D I
authors.initials: DI
authors.lastname: Gulyaev
authors.forename: G
authors.initials: G
authors.lastname: Vergoten
authors.forename: N N
authors.initials: NN
authors.lastname: Modyanov
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000201:enzymology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003198:Computer Simulation; D004563:Electrochemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry*; D012984:Software
chemical_list: D008565:Membrane Proteins; D000254:Sodium-Potassium-Exchanging ATPase