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PubMed · 10329132

A turn propensity scale for transmembrane helices.

M Monné·M Hermansson·G von Heijne
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Abstract

Using a model protein with a 40 residue hydrophobic transmembrane segment, we have measured the ability of all the 20 naturally occurring amino acids to form a tight turn when placed in the middle of the hydrophobic segment. Turn propensities in a transmembrane helix are found to be markedly different from those of globular proteins, and in most cases correlate closely with the hydrophobicity of the residue. The turn propensity scale may be used to improve current methods for membrane protein topology prediction.

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Amino Acid SubstitutionAmino AcidsAnimalsBacterial ProteinsDogsEscherichia coliGlycosylationMembrane ProteinsMicrosomesMutagenesis, Site-DirectedPeptides, CyclicProtein Processing, Post-TranslationalProtein Structure, SecondaryRecombinant Fusion ProteinsComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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M Monné, M Hermansson, G von Heijne. 1999-04-23. A turn propensity scale for transmembrane helices.. https://doi.org/10.1006/jmbi.1999.2657

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