Abstract:
:The macromolecular crowding progressively has been gaining prominence in recent years as it acts as a sword with double-edge on protein stability and folding, i.e., showing assorted results of having both stabilizing and destabilizing effects. We studied the effects of different concentrations of polyethylene glycol (PEG-10) on structure and stability of myoglobin. The tertiary structure of myoglobin was found to be perturbed in the presence of polyethylene glycol, however there was insignificant change in the secondary structure. It was observed that polyethylene glycol induces molten globule state in myoglobin, where the intermediate state holds hydrophobic patches and larger hydrodynamic volume as compared to the native protein. In addition, isothermal titration calorimetry (ITC) showed strong binding between myoglobin and polyethylene glycol, at the physiological pH. We hypothesize that polyethylene glycol induces molten globule conformation in myoglobin by interacting with heme group of myoglobin. We caution that the binding of protein with crowder and other soft interactions need to be gravely well thought-out when studying macromolecular crowding. In our case, destabilizing protein-crowder interactions could compete and overcome the stabilizing exclusion volume effect.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Parray ZA,Shahid S,Ahmad F,Hassan MI,Islam Adoi
10.1016/j.ijbiomac.2017.02.084subject
Has Abstractpub_date
2017-06-01 00:00:00pages
241-248eissn
0141-8130issn
1879-0003pii
S0141-8130(16)33036-7journal_volume
99pub_type
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