Refolding of urea-induced denaturation of model proteins by trimethylamine N-oxide
► We have studied the refolding of urea-induced denaturation of CDs by TMAO. ► We have performed Δ G′ tr and the hydrodynamic diameter ( d H ) of CDs. ► We observed positive values of Δ G′ tr for CDs from water to TMAO. ► The negative Δ G′ tr contributions were obtained for CDs from water to urea. ►...
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| Published in | Thermochimica acta Vol. 526; no. 1; pp. 143 - 150 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford
Elsevier B.V
10.11.2011
Elsevier |
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| Abstract | ► We have studied the refolding of urea-induced denaturation of CDs by TMAO. ► We have performed Δ
G′
tr and the hydrodynamic diameter (
d
H
) of CDs. ► We observed positive values of Δ
G′
tr for CDs from water to TMAO. ► The negative Δ
G′
tr contributions were obtained for CDs from water to urea. ► Our results show that TMAO stabilize while urea destabilizes the CDs. ► Our results show that TMAO is a refolding additive for CDs.
The biomolecules are known to be stabilized by osmolytes, trimethylamine-N-oxide (TMAO) while urea, destabilizes the protein structures. The deleterious effect of urea on proteins has been counteracted by TMAO is well understood; nonetheless, refolding of urea-induced conformational changes of proteins by TMAO is still an active subject. To understand the refolding ability of TMAO from urea-induced denaturation of biomolecules, we have performed transfer free energy (Δ
G′
tr) and the hydrodynamic diameter (
d
H
) of cyclic dipeptides (CDs) such as, cyclo(Gly–Gly), and cyclo(Leu–Ala) through solubilities and dynamic light scattering (DLS) measurements, respectively. We observed positive and negative values of Δ
G′
tr for CDs from water to TMAO and urea, respectively. Our results reveal that TMAO is a refolding additive for urea deleterious actions on CDs at 1:1 and 1:2 molar ratios of TMAO and urea. However, TMAO (1
M) fails to refolding CDs structure from the urea (3–5
M)-induced conformational changes on CDs. |
|---|---|
| AbstractList | The biomolecules are known to be stabilized by osmolytes, trimethylamine-N-oxide (TMAO) while urea, destabilizes the protein structures. The deleterious effect of urea on proteins has been counteracted by TMAO is well understood; nonetheless, refolding of urea-induced conformational changes of proteins by TMAO is still an active subject. To understand the refolding ability of TMAO from urea-induced denaturation of biomolecules, we have performed transfer free energy (ΔG′ₜᵣ) and the hydrodynamic diameter (dH) of cyclic dipeptides (CDs) such as, cyclo(Gly–Gly), and cyclo(Leu–Ala) through solubilities and dynamic light scattering (DLS) measurements, respectively. We observed positive and negative values of ΔG′ₜᵣ for CDs from water to TMAO and urea, respectively. Our results reveal that TMAO is a refolding additive for urea deleterious actions on CDs at 1:1 and 1:2 molar ratios of TMAO and urea. However, TMAO (1M) fails to refolding CDs structure from the urea (3–5M)-induced conformational changes on CDs. ► We have studied the refolding of urea-induced denaturation of CDs by TMAO. ► We have performed Δ G′ tr and the hydrodynamic diameter ( d H ) of CDs. ► We observed positive values of Δ G′ tr for CDs from water to TMAO. ► The negative Δ G′ tr contributions were obtained for CDs from water to urea. ► Our results show that TMAO stabilize while urea destabilizes the CDs. ► Our results show that TMAO is a refolding additive for CDs. The biomolecules are known to be stabilized by osmolytes, trimethylamine-N-oxide (TMAO) while urea, destabilizes the protein structures. The deleterious effect of urea on proteins has been counteracted by TMAO is well understood; nonetheless, refolding of urea-induced conformational changes of proteins by TMAO is still an active subject. To understand the refolding ability of TMAO from urea-induced denaturation of biomolecules, we have performed transfer free energy (Δ G′ tr) and the hydrodynamic diameter ( d H ) of cyclic dipeptides (CDs) such as, cyclo(Gly–Gly), and cyclo(Leu–Ala) through solubilities and dynamic light scattering (DLS) measurements, respectively. We observed positive and negative values of Δ G′ tr for CDs from water to TMAO and urea, respectively. Our results reveal that TMAO is a refolding additive for urea deleterious actions on CDs at 1:1 and 1:2 molar ratios of TMAO and urea. However, TMAO (1 M) fails to refolding CDs structure from the urea (3–5 M)-induced conformational changes on CDs. |
| Author | Attri, Pankaj Venkatesu, Pannuru |
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| Keywords | Transfer free energy Cyclic dipeptides Urea Dynamic light scattering Refolding Trimethylamine-N-oxide Cyclic peptides Light scattering Denaturation Conformational changes Free energy Protein Dipeptides Models Amine oxide Thermodynamic properties Energy transfer |
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| Snippet | ► We have studied the refolding of urea-induced denaturation of CDs by TMAO. ► We have performed Δ
G′
tr and the hydrodynamic diameter (
d
H
) of CDs. ► We... The biomolecules are known to be stabilized by osmolytes, trimethylamine-N-oxide (TMAO) while urea, destabilizes the protein structures. The deleterious effect... |
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| SubjectTerms | Biological and medical sciences Conformational dynamics in molecular biology Cyclic dipeptides denaturation dipeptides Dynamic light scattering energy Fundamental and applied biological sciences. Psychology hydrodynamics light scattering Molecular biophysics proteins Refolding Transfer free energy trimethylamine Trimethylamine-N-oxide Urea |
| Title | Refolding of urea-induced denaturation of model proteins by trimethylamine N-oxide |
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