On the difference in stability between horse and sperm whale myoglobins.
Abstract: The work in the literature on apomyoglobin is almost equally divided between horse and sperm whale myoglobins. The two proteins share high homology, show similar folding behavior, and it is often assumed that all folding phenomena found with one protein will also be found with the other. We report data at equilibrium showing that horse myoglobin was 2.1 kcal/mol less stable than sperm whale myoglobin at pH 5.0, and aggregated at high concentrations as measured by gel filtration and analytical ultracentrifugation experiments. The higher stability of sperm whale myoglobin was identified for both apo and holo forms, and was independent of pH from 5 to 8 and of the presence of sodium chloride. We also show that the substitution of sperm whale myoglobin residues Ala15 and Ala74 to Gly, the residues found at positions 15 and 74 in horse myoglobin, decreased the stability by 1.0 kcal/mol, indicating that helix propensity is an important component of the explanation for the difference in stability between the two proteins.
Publication Date: 2005-03-09 PubMed ID: 15752722DOI: 10.1016/j.abb.2005.01.016Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research compares the stability of myoglobin proteins from horses and sperm whales, finding that sperm whale myoglobin is significantly more stable.
Introduction
- The research focuses on apomyoglobin, a protein found in muscle tissue of both horses and sperm whales. Despite the high similarity between these two proteins, this study found a significant difference in their stability.
- Myoglobin is a type of protein that holds oxygen in muscle cells, aiding in the process of respiration. Researchers often assume that the folding behavior and other characteristics of a protein from one species will be identical in another species if the proteins share high homology (similarity in their structures).
Procedure and Results
- The team tested the stability of the myoglobin proteins from both species at different pH levels (from 5 to 8) and in the presence of sodium chloride. They found that the myoglobin from sperm whales was more stable by 2.1 kcal/mol at pH 5.0.
- In the same conditions, horse myoglobin aggregated at high concentrations as demonstrated through gel filtration and analytical ultracentrifugation experiments.
- The superior stability of sperm whale myoglobin was found in both apo (without a heme group) and holo (with a heme group) forms.
Role of Ala15 and Ala74
- The research further examined the role of specific amino acid residues in the stability of these proteins. They observed that the presence of Glycine (Gly) at positions 15 and 74 in horse myoglobin, instead of Alanine (Ala), decreased the stability of sperm whale myoglobin by 1.0 kcal/mol.
- This indicates that the propensity of a protein helix (a structural element of proteins) contributes significantly to the discrepancy in stability between horse and sperm whale myoglobins.
Conclusion
- Overall, despite the high degree of similarity between horse and sperm whale myoglobins, this research findings suggest a significant difference in the stability of these proteins, with sperm whale myoglobin being more stable.
- They deduced that amino acid residues at specific positions and the propensity of a helix structure in these proteins play a key role in determining their relative stabilities.
Cite This Article
APA
Regis WC, Fattori J, Santoro MM, Jamin M, Ramos CH.
(2005).
On the difference in stability between horse and sperm whale myoglobins.
Arch Biochem Biophys, 436(1), 168-177.
https://doi.org/10.1016/j.abb.2005.01.016 Publication
Researcher Affiliations
- Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Síncrotron, P.O. Box 6192, ZIP Code 13084971, Campinas SP, Brazil.
MeSH Terms
- Animals
- Base Sequence
- Chromatography, Gel
- Dose-Response Relationship, Drug
- Horses
- Hydrogen-Ion Concentration
- Molecular Sequence Data
- Myoglobin / chemistry
- Myoglobin / metabolism
- Protein Denaturation
- Protein Folding
- Species Specificity
- Temperature
- Ultracentrifugation
- Urea / pharmacology
- Whales
Citations
This article has been cited 14 times.- Sackerson C, Garcia V, Medina N, Maldonado J, Daly J, Cartwright R. Comparative analysis of the myoglobin gene in whales and humans reveals evolutionary changes in regulatory elements and expression levels. PLoS One 2023;18(8):e0284834.
- Lubskyy A, Guo C, Chadwick RJ, Petri-Fink A, Bruns N, Pellizzoni MM. Engineered myoglobin as a catalyst for atom transfer radical cyclisation. Chem Commun (Camb) 2022 Sep 29;58(78):10989-10992.
- Guo C, Chadwick RJ, Foulis A, Bedendi G, Lubskyy A, Rodriguez KJ, Pellizzoni MM, Milton RD, Beveridge R, Bruns N. Peroxidase Activity of Myoglobin Variants Reconstituted with Artificial Cofactors. Chembiochem 2022 Sep 16;23(18):e202200197.
- Hasan MM, Ushio H, Ochiai Y. Expression and characterization of rainbow trout Oncorhynchus mykiss recombinant myoglobin. Fish Physiol Biochem 2021 Oct;47(5):1477-1488.
- Wasilewska M, Nattich-Rak M, Pomorska A, Adamczyk Z. Mechanism of Myoglobin Molecule Adsorption on Silica: QCM, OWLS and AFM Investigations. Int J Environ Res Public Health 2021 May 6;18(9).
- Hasan MM, Arafah P, Ozawa H, Ushio H, Ochiai Y. Thermal denaturation and autoxidation profiles of carangid fish myoglobins. Fish Physiol Biochem 2021 Apr;47(2):487-498.
- Mizukami T, Abe Y, Maki K. Evidence for a Shared Mechanism in the Formation of Urea-Induced Kinetic and Equilibrium Intermediates of Horse Apomyoglobin from Ultrarapid Mixing Experiments. PLoS One 2015;10(8):e0134238.
- Mohamad NR, Marzuki NH, Buang NA, Huyop F, Wahab RA. An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes. Biotechnol Biotechnol Equip 2015 Mar 4;29(2):205-220.
- Lerch MT, Horwitz J, McCoy J, Hubbell WL. Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin. Proc Natl Acad Sci U S A 2013 Dec 3;110(49):E4714-22.
- Dasmeh P, Serohijos AW, Kepp KP, Shakhnovich EI. Positively selected sites in cetacean myoglobins contribute to protein stability. PLoS Comput Biol 2013;9(3):e1002929.
- Hasan MM, Watabe S, Ochiai Y. Structural characterization of carangid fish myoglobins. Fish Physiol Biochem 2012 Oct;38(5):1311-22.
- Guo L, Park J, Lee T, Chowdhury P, Lim M, Gai F. Probing the role of hydration in the unfolding transitions of carbonmonoxy myoglobin and apomyoglobin. J Phys Chem B 2009 Apr 30;113(17):6158-63.
- Landfried DA, Vuletich DA, Pond MP, Lecomte JT. Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins. Gene 2007 Aug 15;398(1-2):12-28.
- Ligorio RF, Grosskopf P, Dos Santos LHR, Krawczuk A. Unveiling GruPol: Predicting Electric and Electrostatic Properties of Macromolecules via the Building Block Approach. J Phys Chem B 2024 Aug 22;128(33):7954-7965.
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