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First evidence of formation of pre-molten globule state in myoglobin: A macromolecular crowding approach towards protein folding in vivo.

Abstract：

:Myoglobin is known to show formation of intermediate states under various environmental conditions, in spite of that, this is the first evidence of formation pre-molten globule (PMG) in myoglobin. Polyethylene glycol (PEG) of various molecular sizes shows assorted effects on different proteins. Out of too short and too long PEGs, only PEGs of optimal size interact with proteins leading to change in protein structure that form intermediate state. We are the first one to report the formation of PMG in a protein in the presence of a crowding agent. The PEG-induced intermediate state was characterized by various techniques like absorption, fluorescence, near- and far-UV circular dichroism spectroscopy, ANS binding, and dynamic light scattering measurements to be PMG. Isothermal titration calorimetry and docking studies were further carried out to delineate the mechanism of formation of PMG in myoglobin in physiological conditions. The intermediate formed due to interaction of PEG with myoglobin has physiological implications which are essential to unravel the mystery to solve the massively complicated problems involved in the proper folding of proteins in vivo. Further, outcomes from this study are expected to gain mechanistic insights on the native structure and functions of proteins under in vivo conditions.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

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

doi

10.1016/j.ijbiomac.2018.12.170

subject

Has Abstract

pub_date

2019-04-01 00:00:00

pages

1288-1294

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(18)36095-1

journal_volume

126

pub_type

杂志文章

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