Direct conjugation of semiconductor nanocrystals to a globular protein to study protein-folding intermediates.
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.
Sarkar
Rupa
R
Unit 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.
Narayanan
S Shankara
SS
Pålsson
Lars-Olof
LO
Dias
Fernando
F
Monkman
Andy
A
Pal
Samir Kumar
SK
D019187:Cadmium Compounds / Q000737:chemistry; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D017510:Protein Folding; D045663:Quantum Dots; D012709:Serum Albumin / Q000096:biosynthesis / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013440:Sulfides / Q000737:chemistry
D019187:Cadmium Compounds; D012709:Serum Albumin; D013440:Sulfides; C034939:cadmium sulfide