Speaker
Description
IDPs are identified by the presence of unfolded region due to relatively
abundant polar residues content within its amino acid sequence. Together
with other residues, IDPs exhibit not only high flexibility but
also sensitivity to physico-chemical fluctuation such as pH, temperature,
and ions concentration. For this reason, IDPs are involved in
cellular processes such as DNA repair scheme and chromatin modification.
In this project, we pursue a quantitative description of structure
and dynamics of IDPs with different net charges: namely Prothymosin
Alpha and Myelin Basic Protein. Here, we employed neutron spinecho
spectroscopy (NSE) and small angle X-ray scattering (SAXS) to
gain insight on the emergence of internal friction within the peptide
and its conformational change as a function of Guanidinium Chloride
(GndCl) concentration respectively. The experimental results obtained
from SAXS shows contraction and expansion as measured by FRET.
Similarly, from NSE data, we are able to extract the internal friction
which is in good agreement with FCS results.
