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Acidic residues of protein molecules form electrostatic interactions with these quantum dots (QDs). To determine the stoichiometry of proteins bound to QDs, we used dynamic light scattering (DLS) and zeta potential techniques. Fluorescence resonance energy transfer (FRET) experiments revealed energy transfer from tryptophan residues in the proteins to the QD particles. Quenching of the intrinsic fluorescence of protein molecules was noticed during this binding process (hierarchy HSA&lt;\u03b2\u2010Lg &lt;BSA, lower binding affinity for hydrophobic protein molecules). Upon binding with QD particles, the protein molecules underwent substantial conformational changes at the secondary\u2010structure level (50\u2009% helicity lost), due to loss in hydration.<\/jats:p>","DOI":"10.1002\/cphc.201402629","type":"journal-article","created":{"date-parts":[[2015,3,12]],"date-time":"2015-03-12T17:31:26Z","timestamp":1426181486000},"page":"1777-1786","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Interaction of Globular Plasma Proteins with Water\u2010Soluble CdSe Quantum Dots"],"prefix":"10.1002","volume":"16","author":[{"given":"Jyotsana","family":"Pathak","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kamla","family":"Rawat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shilpa","family":"Sanwlani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H. 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