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Tracking Conformational Changes in Phosvitin throughout a Crowding‐Agent‐Based Titration
Author(s) -
Van de Vondel Evelien,
Herrebout Wouter,
Johannessen Christian
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800581
Subject(s) - phosvitin , macromolecular crowding , protein secondary structure , chemistry , conformational change , circular dichroism , raman optical activity , ficoll , biophysics , folding (dsp implementation) , protein structure , crystallography , structural change , protein folding , biochemistry , phosphorylation , biology , macromolecule , molecule , organic chemistry , peripheral blood mononuclear cell , protein kinase a , electrical engineering , in vitro , engineering , macroeconomics , economics
The sensitivity of Raman optical activity (ROA) towards small conformational changes is explored by tracking the structural changes in an intrinsically disordered protein—phosvitin—induced by different concentrations of crowding agent. It is shown that ROA is capable of tracking small conformational changes involving β‐sheet and α‐helical secondary structural properties of the protein. Furthermore, it is indicated that the influences of the crowding agents employed, Ficoll 70 and dextran 70, on the structural properties of phosvitin differ significantly, with the structural changes induced by the presence of Ficoll 70 being more pronounced and already being visible at a lower concentration. The data also suggest that some spectral changes do not arise from a change in the secondary structure of the protein, but are related to differences in interaction between the phosphorylated residues of the protein and the sugar‐based crowding agent.