ISSN:
1573-4943
Keywords:
Hydrophobicity potential
;
transmembrane helices
;
hairpin structures
;
molecular modeling
;
Na+, K+-ATPase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract 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 ofRhodopseudomonas 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01024971
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