Characterization of acid-induced molten globule like state of ficin

K. B. Devaraj; Parigi Ramesh Kumar; V. Prakash

doi:10.1016/j.ijbiomac.2009.05.008

Characterization of acid-induced molten globule like state of ficin

K. B. Devaraj, Parigi Ramesh Kumar, V. Prakash^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

Abstract

Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about ∼74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography.

Original language	English
Pages (from-to)	248-254
Number of pages	7
Journal	International Journal of Biological Macromolecules
Volume	45
Issue number	3
DOIs	https://doi.org/10.1016/j.ijbiomac.2009.05.008
Publication status	Published - 1 Oct 2009
Externally published	Yes

Keywords

Acid-unfolding
Cysteine protease
Ficin
Molten globule
Protein folding

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10.1016/j.ijbiomac.2009.05.008

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title = "Characterization of acid-induced molten globule like state of ficin",

abstract = "Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about ∼74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography.",

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AU - Devaraj, K. B.

AU - Kumar, Parigi Ramesh

AU - Prakash, V.

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Y1 - 2009/10/1

N2 - Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about ∼74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography.

AB - Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about ∼74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography.

KW - Acid-unfolding

KW - Cysteine protease

KW - Ficin

KW - Molten globule

KW - Protein folding

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DO - 10.1016/j.ijbiomac.2009.05.008

M3 - Article

C2 - 19482042

AN - SCOPUS:67651033247

SN - 0141-8130

VL - 45

SP - 248

EP - 254

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

IS - 3

ER -

Characterization of acid-induced molten globule like state of ficin

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Keywords

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