ISSN:
1432-2234
Schlagwort(e):
Key words: Hydrophobic interactions
;
Molecular modeling
;
Molecular hydrophobicity potential
;
Helix-helix contacts
;
Protein fold recognition
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Chemie und Pharmazie
Notizen:
Abstract. We present a “hydrophobic template” method enabling recognition of α-helix bundles in membrane channels from sequence analysis. Inspection of hydrophobic properties of pore-forming helices in proteins with known structure (A-B5 toxins) permits delineation of a common polarity motif: two hydrophobic surface stretches separated by polar areas. The bundles are stabilized by nonpolar interhelical contacts. A number of transmembrane segments were checked for presence of this motif, and it was detected for pore-forming helices of several ion transporters (segments M2 of acetylcholine and GABAA receptors, α5 peptide of δ-endotoxin), which reveal five α-helix bundle architecture. Applications of the method to modeling of membrane channels are discussed.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/s002140050409
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