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Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
Direct conjugation of semiconductor nanocrystals to a globular protein to study protein-folding intermediates
Rupa Sarkar1, S Shankara Narayanan, Lars-Olof Pålsson
1Unit for Nano Science & Technology, Department of Chemical, Biological & Macromolecular Sciences, S. N. Bose National Centre for Basic Sciences, Block JD, Sector III, Salt Lake, Kolkata 700 098, India.
Abstract:
In this Article, we study the development of semiconductor nanocrystals (quantum dots of average diameter less than 2 nm) directly conjugated to a transporter protein human serum albumin (HSA) as fluorescent biological labels. Förster resonance energy transfer (FRET) from the amino acid tryptophan (Trp214) to quantum dot in HSA is monitored to follow the local and global changes in the protein structure during thermal unfolding and refolding processes. This study is likely to attract widespread attention as a powerful tool for the study of protein folding.
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