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Module 6.4 · Topic 7
Module 6.4 · Topic 7
Predicting a shape nobody has actually solved yet
A few lessons back, Proline's rigid ring structure explained why substituting it into a sequence earns a steep penalty in alignment scoring. That same chemical fact turns out to be useful for a completely different purpose — predicting, from sequence alone, where a protein's structure is likely to break.
Certain amino acids show a strong statistical preference for forming alpha helices; others favour beta sheets; Proline, due to its rigid ring, strongly disfavours both. Could scanning an unsolved sequence for these known propensities predict its likely secondary structure?
Secondary structure prediction methods rely on:
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