Variation in the structural changes of myoglobin in the presence of several protic ionic liquid

Pankaj Attri, Indrani Jha, Eun Ha Choi, Pannuru Venkatesu

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Protein stability in ionic solution depends on the delicate balance between protein-ion and ion-ion interactions. To address the ion specific effects on the protein, we have examined the stability of myoglobin (Mb) in the presence of buffer and ammonium-based ionic liquids (ILs) (50%, v/v). Here, fluorescence and circular dichroism (CD) spectroscopy experiments are used to study the influence of ILs on structure and stability of Mb. Our experimental results reveal that more viscous ILs (sulphate or phosphate ions) are stabilizers and therefore more biocompatible for Mb structure. Surprisingly, the less viscous ILs such as acetate anion based ILs are destabilizers for the native structure of Mb. Our results explicitly elucidate that anion variation has significant influence on Mb stability efficiency than cation variation. This study provides insight into anion effects on protein stability and explains that the intrasolvent interactions can be leveraged to enhance the stability.

Original languageEnglish
Pages (from-to)114-123
Number of pages10
JournalInternational Journal of Biological Macromolecules
Volume69
DOIs
Publication statusPublished - Aug 2014

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Ionic Liquids
Myoglobin
Ionic liquids
Ions
Anions
Protein Stability
Proteins
Negative ions
Circular dichroism spectroscopy
Circular Dichroism
Ammonium Compounds
Sulfates
Cations
Spectrum Analysis
Buffers
Acetates
Fluorescence
Phosphates
Structural change
Positive ions

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)

Cite this

Variation in the structural changes of myoglobin in the presence of several protic ionic liquid. / Attri, Pankaj; Jha, Indrani; Choi, Eun Ha; Venkatesu, Pannuru.

In: International Journal of Biological Macromolecules, Vol. 69, 08.2014, p. 114-123.

Research output: Contribution to journalArticle

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