A turn propensity scale for transmembrane helices.
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.
D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D004285:Dogs; D004926:Escherichia coli / Q000737:chemistry; D006031:Glycosylation; D008565:Membrane Proteins / Q000737:chemistry; D008861:Microsomes / Q000648:ultrastructure; D016297:Mutagenesis, Site-Directed; D010456:Peptides, Cyclic / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry