A size dependent folding contour for cytochrome C

A size dependent folding contour for cytochrome C
Received 7 July 2005; revised 20 August 2005; accepted 22 August 2005. Available online 23 September 2005.
Shibsekhar Roy, Santiswarup Singha, Jaydeep Bhattacharya, Ranjita GhoshMoulick and Anjan Kr. Dasgupta
Biophysical Chemistry
Volume 119, Issue 1 , 1 January 2006
Department of Biochemistry, Calcutta University, Kolkata, 700019, India
The paper describes an experimental construct of the folding route of the heme protein cytochrome-C. The construct highlights a slowing down near the nose of the folding funnel caused by the multiplicity of the energy traps near the native conformation created as a result of complex hemeÒpeptide interaction. Interestingly the hydrodynamic size, the size heterogeneity and peroxidase activity serve as a triple measure of the distance of this near equilibrium departure from native conformation. Accordingly, the folding process is marked with a gradual and reversible reduction of mean hydrodynamic size, size heterogeneity and peroxidase activity (higher in unfolded state). The Dynamic Light Scattering based straightforward illustration of hydrodynamic size variation may serve as a model to slow folding observed in case of heme proteins, the heme itself serving as a natural facilitator for the native peptide conformation.
Keywords: Cytochrome-C; Hydrodynamic size; Size heterogeneity; Dynamic Light Scattering
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