Abstract
A simple spectrophotometric approach is proposed for sensing coil-to-helix and helix-to-coil conformational transitions of intrinsically disordered and folded peptide/protein sequences. Helix formation induced by a variety of physico-chemical factors results in a substantial intensity reduction (hypochromism) of the intense far-UV absorption band associated with the π-π* transition of amide chromophores. Conversely, the same band exhibits intensity increase (hyperchromism) as the consequence of unfolding events. This method, faded into obscurity several decades ago, may obtain widespread applications in the field of protein science.
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