Abstract
The first solved protein structures were helical globular proteins and soon after their availability for structural analysis, it was noted that buried surfaces of α-helices were composed of hydrophobic residues. Schiffer and Edmundson (1967) introduced the helical wheel representation, in which residues are positioned at 100° intervals around a circle (i.e. 3.6 residues per turn) and suggested its use as a predictive tool for helices. Given the variability of helical length and degree of burial in the tertiary structure, the use of this tool alone proved too simplistic and the presence or absence of helices could not be predicted with a high degree of certainty. Nevertheless, the frequent use of helical wheels to plot segments of sequence with good helical amphipathicity testifies to the continuing utility of this simple representation.
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Gibson, T.J. (1992). Assignment of α-Helices in Multiply Aligned Protein Sequences — Applications to DNA Binding Motifs. In: Taylor, W.R. (eds) Patterns in Protein Sequence and Structure. Springer Series in Biophysics, vol 7. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76637-4_10
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DOI: https://doi.org/10.1007/978-3-642-76637-4_10
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