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Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/906

Title: Direct observation of protein folding in nanoenvironments using a molecular ruler
Authors: Sarkar, Rupa
Shaw, Ajay Kumar
Shankara Narayanan, S
Dias, Fernando
Monkman, Andy
Pal, Samir Kumar
Keywords: Cytochrome c
Protein folding
Micelles and reverse micelles
Picosecond dynamics
Time-resolved fluorescence anisotropy
Circular dichroism spectroscopy
Issue Date: 2006
Publisher: Biophysical Chemistry
Citation: R. Sarkar, A. K. Shaw, S. S. Narayanan, F. Dias, A. Monkman and S. K. Pal, Direct Observation of Protein Folding in Nanoenvironments using a Molecular Ruler, Biophysical Chemistry 123 (2006) 40.
Abstract: We observe folding of horse heart cytochrome c in various environments including nano-compartments (micelles and reverse micelles). Using picosecond-resolved Förster resonance energy transfer (FRET) dynamics of an extrinsic covalently attached probe dansyl (donor) at the surface of the protein to a heme group (acceptor) embedded inside the protein, we measured angstrom-resolved donor–acceptor distances in the environments. The overall structural perturbations of the protein revealed from the FRET experiments are in close agreement with our circular dichroism (CD) and dynamic light scattering (DLS) studies on the protein in a variety of solution conditions. The change of segmental motion of the protein due to imposed restriction in the nano-compartments compared to that in bulk buffer is also revealed by temporal fluorescence anisotropy of the dansyl probe.
URI: http://hdl.handle.net/123456789/906
Appears in Collections:2006

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