A size dependent folding contour for cytochrome C.
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 heme-peptide 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.
Roy
Shibsekhar
S
Department of Biochemistry, Calcutta University, Kolkata, 700019, India.
Singha
Santiswarup
S
Bhattacharya
Jaydeep
J
Ghoshmoulick
Ranjita
R
Dasgupta
Anjan Kr
AK
D001665:Binding Sites; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism; D006418:Heme / Q000737:chemistry*; D008970:Molecular Weight; D009195:Peroxidase / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D020673:Protein Renaturation; D012542:Scattering, Radiation
D006418:Heme; D045304:Cytochromes c; D009195:Peroxidase