Mechanism for stabilization of the molten globule state of papain by sodium n-alkyl sulfates: Spectroscopic and calorimetric approaches

Chamani, Jamshidkhan; Heshmati, Masoumeh

doi:10.1016/j.jcis.2008.03.001

Cited by 75 publications

(34 citation statements)

References 58 publications

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“…These observations further suggest that acid-induced state becomes a compact molecule with the exposure of hydrophobic clusters. All the above characteristics are typical of a MG state observed with several proteins [7,[18][19][20][21].…”

Section: Resultsmentioning

confidence: 53%

“…Hence it is crucial to identify and define the partially folded structures to understand the principles governing protein folding and stability. A considerable amount of efforts have been currently devoted to identify and study the partially folded structures of proteins [17][18][19][20][21]29]. It is now accepted that proteins are known to acquire different conformational intermediate states during unfolding by various denaturing agents [8][9][10]30].…”

Section: Resultsmentioning

confidence: 99%

“…The available information indicates that ficin apparently shares many common properties with papain [16]. The extensive studies on the folding pathways of papain as well as other related cysteine proteases are well established [10,[17][18][19][20][21], however a very little information on structural aspects of ficin is available till date. The investigations on conformational behaviours of the similar proteases from different sources of cysteine proteases family would certainly help in understanding the folding pathway of these proteases.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of acid-induced molten globule like state of ficin

Devaraj¹,

Kumar²,

Prakash³

2009

International Journal of Biological Macromolecules

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Section: Resultsmentioning

confidence: 53%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of acid-induced molten globule like state of ficin

Devaraj¹,

Kumar²,

Prakash³

2009

International Journal of Biological Macromolecules

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“…The molten globule state is a common equilibrium intermediate between native and unfolded states for many proteins in both directions of folding and unfolding transitions [7,[40][41][42][43][44][45][46][47][48]. Processes in which molten globule states are believed to participate include translocation of proteins across membranes, protein-protein interactions, and protein degradation [49].…”

Section: Discussionmentioning

confidence: 99%

Characterization of Acid-Induced Partially Folded Conformation Resembling a Molten Globule State of Polygalacturonase from a Filamentous Fungus Tetracoccosporium sp.

Aminzadeh

Naderi-Manesh

Khajeh

et al. 2009

Appl Biochem Biotechnol

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Acid-induced unfolding of a Tetracoccosporium sp. polygalacturonase enzyme (PG) was studied by a comprehensive series of biophysical and biochemical techniques. At pH 1.0, PG acquires partially folded state, which reveals characteristics of molten globule (MG) state, i.e., reduction of defined tertiary structure with minimal changes in the secondary structure. In this study PG unfolds exposing its hydrophobic surface to a greater extent than the native form at acidic pH with more tryptophan residues exposed to the solvent. Collectively, our data imply the presence of MG state of PG at low pH, suggesting the phenomenon of hydrophobic collapse model for folding and integration into cell membrane.

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“…8-Anilino-1-naphthalen sulfonic acid (ANS) was purchased from Aldrich-Sigma, USA. A stock solution of ANS was prepared in minimum amount of methanol and the concentration was determined with an extinction coefficient of 5000 M -1 cm -1 at 380 nm [27]. All other used reagents were of analytical grade, the highest quality commercially available.…”

Section: Methodsmentioning

confidence: 99%

Thermodynamic Study of Intermediate State of Papain Induced by n-Alkyl Sulfates at Two Different pH Values: A Spectroscopic Approach

Chamani¹,

Heshmati²,

Rajabi³

et al. 2009

TOSURSJ

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Abstract:The formation of the intermediate state of papain was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; and sodium dodecyl sulfate, SDS at different concentrations. A systematic investigation of n-alkyl sulfates induced conformational alteration in molten globule state under an acidic condition and the native state of papain was examined by tryptophan fluorescence, 1-anilino 8-naphtalene sulfonic acid (ANS) binding and UV absorbance. The addition of n-alkyl sulfates to molten globule state at pH 2 shows a decrease in tryptophan fluorescence intensity and quenched ANS fluorescence relative to the native state that leads to enhancement in tryptophan fluorescence and an increase in ANS fluorescence as well. In the presence of n-alkyl sulfates in various conditions, two intermediate (I A and I B ) with different conformations were obtained at acidic and native states, respectively. Thus, we can assume that the intermediate states in folding and unfolding pathways in various conditions have different structures. The results show that SDS is much more effective than SDeS and SOS for the formation of the intermediate states for papain in the two different pathways due to the presence of its hydrophobic tail. Therefore, hydrophobic interactions play an important role in inducing the two different intermediates along the two various thermodynamic pathways.

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Mechanism for stabilization of the molten globule state of papain by sodium n-alkyl sulfates: Spectroscopic and calorimetric approaches

Cited by 75 publications

References 58 publications

Characterization of acid-induced molten globule like state of ficin

Characterization of acid-induced molten globule like state of ficin

Characterization of Acid-Induced Partially Folded Conformation Resembling a Molten Globule State of Polygalacturonase from a Filamentous Fungus Tetracoccosporium sp.

Thermodynamic Study of Intermediate State of Papain Induced by n-Alkyl Sulfates at Two Different pH Values: A Spectroscopic Approach

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