Abstract:
:Structural changes in R-phycoerythrin used as a matrix for the synthesis of CdS quantum dots have been analyzed by circular dichroism spectrometry. In deionized water, quantum dot synthesis in the tunnel cavity of the R-phycoerythrin molecule proved to be accompanied by uncoiling of α-helices and changes in the conformation of its chromophore groups, with consequent decay of protein fluorescence. Since R-phycoerythrin fluorescence is important for practical applications, conditions for quantum dot synthesis have been optimized by replacing deionized water with 0.01 M MES buffer, pH 5.7. Under such conditions, the size of the CdS quantum dots (determined from atomic force microscopy images) remains the same as in deionized water, but quantum dots cause only minor structural changes in protein molecules, as follows from circular dichroism and absorption spectra. The thermostability of R-phycoerythrin is enhanced, as indicated by an increase in the experimental activation energy for denaturation (from 140.8 to 149.9 kJ/mol) and the intensity of R-phycoerythrin fluorescence is also enhanced approximately twofold.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Bekasova OD,Shubin VV,Safenkova IV,Kovalyov LI,Kurganov BIdoi
10.1016/j.ijbiomac.2013.10.010subject
Has Abstractpub_date
2013-11-01 00:00:00pages
623-8eissn
0141-8130issn
1879-0003pii
S0141-8130(13)00554-0journal_volume
62pub_type
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