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ITC results proved that NAC\u2010CdTe QDs can spontaneously bind with lysozyme and hydrophobic force plays a major role in stabilizing QDs\u2013lysozyme complex. Multi\u2010spectroscopic measurements revealed that NAC\u2010CdTe QDs caused strong quenching of the lysozyme's fluorescence in a size\u2010dependent quenching manner. Moreover, the changes of secondary structure and microenvironment in lysozyme caused by the NAC\u2010CdTe QDs were higher with a bigger size. The results of enzyme activity assays showed that the interaction between lysozyme and NAC\u2010CdTe QDs inhibited the activity of lysozyme and the inhibiting effect was in a size\u2010dependent manner. Based on these results, we conclude that NAC\u2010CdTe QDs with larger particle size had a larger impact on the structure and function of lysozyme.<\/jats:p>","DOI":"10.1002\/jbt.21982","type":"journal-article","created":{"date-parts":[[2017,9,13]],"date-time":"2017-09-13T13:16:44Z","timestamp":1505308604000},"source":"Crossref","is-referenced-by-count":6,"title":["Spectroscopic investigations on the conformational changes of lysozyme effected by different sizes of N\u2010acetyl\u2010<scp>l<\/scp>\u2010cysteine\u2010capped CdTe quantum dots"],"prefix":"10.1002","volume":"31","author":[{"given":"Qianqian","family":"Wu","sequence":"first","affiliation":[{"name":"School of Environmental Science and Engineering, Shandong University China\u2013America CRC for Environment &amp; Health  Shandong Province Jinan 250100 People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jingqiang","family":"Wan","sequence":"additional","affiliation":[{"name":"School of 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