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Folding of apominimyoglobin

G De Sanctis¹, F Ascoli, M Brunori

¹Dipartimento di Biologia Molecolare, Cellulare e Animale, Università di Camerino, Italy.

Proceedings of the National Academy of Sciences of the United States of America

|November 22, 1994

Summary

The acid unfolding pathway of apominimyoglobin (apo-mini-Mb) shows a folding intermediate similar to native apomyoglobin, despite lacking key helical structures. This suggests apo-mini-Mb may utilize an alternative folding pathway.

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Area of Science:

Protein folding and stability
Biophysical chemistry
Structural biology

Background:

Apomyoglobin (apo-Mb) unfolding pathways are crucial for understanding protein stability.
A partly folded intermediate is observed in sperm whale apomyoglobin at acidic pH.
This intermediate is proposed to involve tertiary interactions between helices A, G, and H.

Purpose of the Study:

To investigate the acid unfolding pathway of apominimyoglobin (apo-mini-Mb), a fragment of horse heart apomyoglobin.
To compare the folding intermediate of apo-mini-Mb with that of native apomyoglobin.
To determine the role of specific helical structures in the folding pathway.

Main Methods:

Circular dichroism spectroscopy was used to study protein structure.
Acid-induced unfolding was performed on both native and apo-mini-Mb.
The effect of trifluoroethanol (TFE) on the unfolding pathway was examined.

Main Results:

A folding intermediate with approximately 33% alpha-helical content was observed for apo-mini-Mb at pH 4.3-5.0.
This intermediate is structurally similar to the one found in native horse heart apomyoglobin.
The helix-stabilizing compound 15% trifluoroethanol similarly affected the unfolding pathways of both native and mini apoproteins.

Conclusions:

Apominimyoglobin (apo-mini-Mb) populates a folding intermediate similar to native apomyoglobin, despite lacking helices A and most of H.
The results suggest that apo-mini-Mb may acquire its folded state through an alternative pathway.
This alternative pathway might also be involved in the folding of native apomyoglobin.

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