Characterization of intermediate state of myoglobin in the presence of PEG 10 under physiological conditions.

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 Macromol

authors

Parray ZA,Shahid S,Ahmad F,Hassan MI,Islam A

doi

10.1016/j.ijbiomac.2017.02.084

subject

Has Abstract

pub_date

2017-06-01 00:00:00

pages

241-248

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(16)33036-7

journal_volume

99

pub_type

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