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We measured the THz absorption coefficient (<jats:italic>\u03b1<\/jats:italic>) of the protein solutions, and it was observed that <jats:italic>\u03b1<\/jats:italic> fluctuated periodically as a function of alcohol concentration at a fixed protein concentration. For a fixed alcohol concentration, an increase in the protein concentration resulted in nonmonotonic changes in <jats:italic>\u03b1<\/jats:italic>; thus, it first decreased rapidly and then increased, which was followed by a shallow decrease. An alcohol\u2010induced \u03b1 helix to random coil transition of the protein secondary structure was revealed by circular dichroism spectroscopy measurements, and the effect was most prominent in TBA. The anomalous change in the hydration was found to be a delicate balance between the various interactions present in the three\u2010component system.<\/jats:p>","DOI":"10.1002\/cphc.201601217","type":"journal-article","created":{"date-parts":[[2017,3,1]],"date-time":"2017-03-01T09:06:38Z","timestamp":1488359198000},"page":"749-754","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Nonmonotonic Hydration Behavior of Bovine Serum Albumin in Alcohol\/Water Binary Mixtures: A Terahertz Spectroscopic Investigation"],"prefix":"10.1002","volume":"18","author":[{"given":"Dipak Kumar","family":"Das","sequence":"first","affiliation":[{"name":"Department of Chemical, Biological and Macromolecular Sciences S. N. 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