2020
DOI: 10.1021/acs.jpcb.0c06247
|View full text |Cite
|
Sign up to set email alerts
|

Cryo vs Thermo: Duality of Ethylene Glycol on the Stability of Proteins

Abstract: Osmolytes are known to stabilize proteins under stress conditions. Thermal denaturation studies on globular proteins (β-lactoglobulin, cytochrome c, myoglobin, α-chymotrypsin) in the presence of ethylene glycol (EG), a polyol class of osmolyte, demonstrate a unique property of EG. EG stabilizes proteins against cold denaturation and destabilizes them during heat-induced denaturation. Further, chemical denaturation experiments performed at room temperature and at a sub-zero temperature (−10 °C) show that EG sta… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

4
11
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
8

Relationship

1
7

Authors

Journals

citations
Cited by 14 publications
(16 citation statements)
references
References 79 publications
4
11
0
Order By: Relevance
“…S9, ESI†), which can explain the energetics of the osmolyte-induced effect on the stabilization/destabilization of the protein. 68,69 The plot (Fig. 11) clearly indicates that the destabilization of ILs is enthalpy-driven in all cases.…”
Section: Discussionmentioning
confidence: 94%
“…S9, ESI†), which can explain the energetics of the osmolyte-induced effect on the stabilization/destabilization of the protein. 68,69 The plot (Fig. 11) clearly indicates that the destabilization of ILs is enthalpy-driven in all cases.…”
Section: Discussionmentioning
confidence: 94%
“…The behavior of protein under thermal perturbation and the impact of cosolvent have been widely studied by molecular dynamics (MD) simulations. It was revealed through MD simulations that the unfolding process of lysozyme induced by high temperature begins in the highly flexible interdomain loop region. , As indicated in previous works, the osmolyte TMAO enhances the stability of lysozyme by altering the structure of bulk water. , A high concentration of TMAO (∼1000 mM) is required to sufficiently strengthen the hydrogen-bond network of aqueous solutions, thereby stabilizing protein. However, there has been limited work on the interactions between ATP and protein, leaving the molecular mechanism underlying how ATP enhances the protein stability with such great efficiency largely obscure.…”
Section: Introductionmentioning
confidence: 99%
“…41). The generalized van't Hoff equation used by these authors is based on eqn ( 17)- (19). Moreover, the dependence of the free energy of unfolding is assumed to be linear in c s as derived above in eqn (13):…”
Section: Theorymentioning
confidence: 99%
“…8 There are many investigations that study the change of T m in the presence of various salts and non-charged solutes which can stabilize or destabilize the globular state. 4,6,7,[9][10][11][12][13][14][15][16][17][18][19][20] This effect is of obvious biological importance and can be traced back to hydration effects embodied in the Hofmeister series. [21][22][23][24] The collapse transition of poly(n-isopropylacrylamide) (PNIPAM) in aqueous solution is another well-studied and fundamental problem where a coiled polymer undergoes a transition from the coiled to the globular state with raising temperature.…”
Section: Introductionmentioning
confidence: 99%