Transmembrane and water-soluble helix bundles display reverse patterns of surface roughness.
Amino acid exposure and surface roughness were calculated for 12 helices from three transmembrane alpha-helix bundles and 13 helices from seven water-soluble alpha-helix bundles. Transmembrane helix bundles have relatively rough surfaces exposed to the lipid bilayer hydrocarbon chains and relatively smooth surfaces along helix-helix interfaces. This pattern is the reverse of what occurs in water-soluble helix bundles, where relatively rough surfaces are at the helix-helix interfaces and relatively smooth surfaces are exposed to water. The relatively rough exposed surfaces and buried smooth surfaces of transmembrane helices are likely to contribute to the stability of transmembrane helical bundles in a phospholipid environment.
Renthal
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Division of Life Sciences, University of Texas at San Antonio, San Antonio, Texas 78249, USA. Rrenthal@UTSA.edu
D003576:Electron Transport Complex IV / Q000737:chemistry; D005583:Fourier Analysis; D017709:Fractals; D006422:Hemerythrin / Q000031:analogs & derivatives / Q000737:chemistry; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry*; D010231:Paracoccus denitrificans / Q000201:enzymology; D017433:Protein Structure, Secondary; D016760:Proto-Oncogene Proteins c-fos / Q000737:chemistry; D016755:Proto-Oncogene Proteins c-jun / Q000737:chemistry; D012995:Solubility
D006422:Hemerythrin; D046911:Macromolecular Substances; D008565:Membrane Proteins; D016760:Proto-Oncogene Proteins c-fos; D016755:Proto-Oncogene Proteins c-jun; C008571:myohemerythrin; D003576:Electron Transport Complex IV