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Home / Equine Research Bank / Biophys J / Determination of the volume changes for pressure-induced tra...
Biophysical journal1998; 75(1); 463-470; doi: 10.1016/S0006-3495(98)77534-4

Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states.

Abstract: The volume change for the transition from the native state of horse heart apomyoglobin to a pressure-induced intermediate with fluorescence properties similar to those of the well-established molten globule or I form was measured to be -70 ml/mol. Complete unfolding of the protein by pressure at pH 4.2 revealed an upper limit for the unfolding of the intermediate of -61 ml/mol. At 0.3 M guanidine hydrochloride, the entire transition from native to molten globule to unfolded state was observed in the available pressure range below 2.5 kbar. The volume change for the N-->I transition is relatively large and does not correlate well with the changes in relative hydration for these transitions derived from measurements of the changes in heat capacity, consistent with the previously observed lack of correlation between the m-value for denaturant-induced transitions and the measured volume change of unfolding for cooperativity mutants of staphylococcal nuclease (Frye et al. 1996. Biochemistry. 35:10234-10239). Our results support the hypothesis that the volume change associated with the hydration of protein surface upon unfolding may involve both positive and negative underlying contributions that effectively cancel, and that the measured volume changes for protein structural transitions arise from another source, perhaps the elimination of void volume due to packing defects in the structured chains.
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Publication Date: 1998-07-02 PubMed ID: 9649407PubMed Central: PMC1299719DOI: 10.1016/S0006-3495(98)77534-4Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research investigates the volume changes during the pressure-induced transitions of the protein apomyoglobin from its native state to intermediate and unfolded states. It was found that the volume changes for these transitions do not align well with hydrating changes, suggesting different sources for these structural changes.

Objective of the Research

  • The aim of the study was to determine the volume changes that occur when horse heart apomyoglobin transitions from its native state to a pressure-induced intermediate state, similar to the molten globule or I form of the protein, and when it is completely unfolded under pressure.

Methodology and Findings

  • The volume change between the native state of apomyoglobin and the intermediate I form was measured to be -70 ml/mol.
  • The upper limit for the complete unfolding of the protein by pressure at pH 4.2 was measured as -61 ml/mol.
  • At 0.3 M guanidine hydrochloride, the full transition from the native state to the molten globule to the unfolded state was observed under pressures below 2.5 kbar.
  • The researchers found that the volume change for the transition from the native state to the intermediate state is relatively large and does not align well with the expected changes in relative hydration based on heat capacity measurements.

Implications and Interpretation

  • The larger volume change for the N–>I transition contradicts the correlations observed in previous studies, such as the lack of correlation between the m-value for denaturant-induced transitions and the measured volume changes of unfolding for cooperativity mutants of staphylococcal nuclease.
  • The study supports the hypothesis that the volume change associated with protein surface hydration upon unfolding can involve both positive and negative contributions, which may effectively cancel out.
  • Therefore, the measured volume changes observed during protein structural transitions might not originate from the changes in hydration but could be due to other factors, such as the elimination of void volumes resulting from packing defects in the structured chains of the protein.

Cite This Article

APA
Vidugiris GJ, Royer CA. (1998). Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states. Biophys J, 75(1), 463-470. https://doi.org/10.1016/S0006-3495(98)77534-4

Publication

Biophysical journal
ISSN: 0006-3495
NlmUniqueID: 0370626
Country: United States
Language: English
Volume: 75
Issue: 1
Pages: 463-470

Researcher Affiliations

Vidugiris, G J
  • School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Royer, C A

    MeSH Terms

    • Animals
    • Apoproteins / chemistry
    • Biophysical Phenomena
    • Biophysics
    • Horses
    • Hydrogen-Ion Concentration
    • Hydrostatic Pressure
    • In Vitro Techniques
    • Myocardium / chemistry
    • Myoglobin / chemistry
    • Protein Conformation
    • Protein Denaturation
    • Protein Folding
    • Spectrometry, Fluorescence

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