Disulfide bonds play crucial roles in biology. Intramolecular disulfide bonds between cysteine residues stabilise folded conformations in proteins, contribute to enzyme and antibiotic activities, and very recently they have been found to act as conformational switches that can activate biological activity in proteins. However, very limited accurate information is available on the conformations around disulfide bonds sampled by proteins and their preferences and influence on reactivity. The aim of this project is to characterise the possible conformational arrangements and reaction pathways of molecular systems involving disulfide bonds by using a combination of advanced high-resolution spectroscopic and biophysical techniques.
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