Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study.
Abstract: A proton nuclear magnetic resonance spectroscopic study of horse apomyoglobin was undertaken in order to define the regions of myoglobin that are and that are not structurally affected by the binding of the prosthetic group. It was found that, in spite of the poor spectral resolution, a number of spin systems could be identified by using standard correlated methods. Four clusters consisting mostly of hydrophobic residues were detected by nuclear Overhauser spectroscopy, two of which involved the tryptophan side chains. Extensive similarities to nuclear Overhauser spectroscopy data collected on the carbonmonoxy form of holomyoglobin suggested tentative assignments for several residues. It appeared that distinct cores of side chains on the distal side of the binding pocket and between the A, B, G, and H helices maintain the same packing as they do in holomyoglobin and apomyoglobin reconstituted with protoporphyrin IX.
Publication Date: 1990-12-18 PubMed ID: 2176892DOI: 10.1021/bi00502a008Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research studies the internal structures of a protein (horse apomyoglobin) using a specific analytical method called proton nuclear magnetic resonance spectroscopy. It identifies parts of the protein which are affected by the binding of a certain group, and observes four clusters of mainly hydrophobic residues, two of which involve specific side chains.
Objective of Research
- The primary goal of this research was to identify the regions of the myoglobin protein (specifically horse apomyoglobin) that are affected by the binding of its prosthetic group using proton nuclear magnetic resonance spectroscopy, a standard analytical technique.
Methodology and Findings
- The researchers used the standard correlated methods for the proton NMR spectroscopy analysis. This helped them to counteract the challenge of poor spectral resolution.
- The analysis unveiled that there were four clusters primarily made up of hydrophobic residues. Hydrophobic residues are portions of proteins that tend to repel or fail to mix with water, thus playing crucial roles in protein folding and stability.
- Two of these four clusters involved the side chains of tryptophan, an essential amino acid.
Comparative Analysis and Interpretations
- The scientists compared the results of this study with the findings from nuclear Overhauser spectroscopy data on carbonmonoxy form of holomyoglobin. The similarities between the data suggested potential assignments for several residues.
- As per the interpretation, the research determined that certain core side chains on the distal side of the binding pocket (region where a ligand – a molecule that binds to another – binds to a protein) and between the A, B, G, and H helices (spiral structures in proteins) of the myoglobin maintain the same packing in different forms of myoglobin – holomyoglobin, apomyoglobin, and reconstituted apomyoglobin with protoporphyrin IX.
Scientific Impact of Research
- This research provides valuable insights into the structural effects of the binding of the prosthetic group to myoglobin. Understanding these effects is key to comprehending the function and behaviour of proteins in biological systems.
- The confirmation of maintained packing across different forms can help in predicting protein behaviour and interactions, thus contributing to the broader understanding of protein science.
Cite This Article
APA
Cocco MJ, Lecomte JT.
(1990).
Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study.
Biochemistry, 29(50), 11067-11072.
https://doi.org/10.1021/bi00502a008 Publication
Researcher Affiliations
- Department of Chemistry, Pennsylvania State University, University Park 16802.
MeSH Terms
- Amino Acid Sequence
- Animals
- Apoproteins / chemistry
- Deuterium
- Deuterium Oxide
- Horses
- Magnetic Resonance Spectroscopy / methods
- Molecular Sequence Data
- Myoglobin / chemistry
- Protein Binding
- Protein Conformation
- Protons
- Water
Citations
This article has been cited 17 times.- Nye DB, Lecomte JTJ. Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin. Biochemistry 2018 Oct 9;57(40):5785-5796.
- Zhang D, Lazim R. Application of conventional molecular dynamics simulation in evaluating the stability of apomyoglobin in urea solution. Sci Rep 2017 Mar 16;7:44651.
- Childers MC, Daggett V. Insights from molecular dynamics simulations for computational protein design. Mol Syst Des Eng 2017 Feb 1;2(1):9-33.
- Dickson CF, Jacques DA, Clubb RT, Guss JM, Gell DA. The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket. Acta Crystallogr D Biol Crystallogr 2015 Jun;71(Pt 6):1295-306.
- Goodman JS, Chao SH, Pogorelov TV, Gruebele M. Filling up the heme pocket stabilizes apomyoglobin and speeds up its folding. J Phys Chem B 2014 Jun 19;118(24):6511-8.
- Feng R, Konishi Y. Stepwise refolding of Acid-denatured myoglobin: Evidence from electrospray mass spectrometry. J Am Soc Mass Spectrom 1993 Aug;4(8):638-45.
- Culbertson DS, Olson JS. Role of heme in the unfolding and assembly of myoglobin. Biochemistry 2010 Jul 27;49(29):6052-63.
- Maguid S, Fernandez-Alberti S, Ferrelli L, Echave J. Exploring the common dynamics of homologous proteins. Application to the globin family. Biophys J 2005 Jul;89(1):3-13.
- Rose GD. Lysozyme among the Lilliputians. Proc Natl Acad Sci U S A 2000 Jan 18;97(2):526-8.
- Abbruzzetti S, Crema E, Masino L, Vecli A, Viappiani C, Small JR, Libertini LJ, Small EW. Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump. Biophys J 2000 Jan;78(1):405-15.
- Lecomte JT, Sukits SF, Bhattacharya S, Falzone CJ. Conformational properties of native sperm whale apomyoglobin in solution. Protein Sci 1999 Jul;8(7):1484-91.
- Robinson CR, Liu Y, O'Brien R, Sligar SG, Sturtevant JM. A differential scanning calorimetric study of the thermal unfolding of apo- and holo-cytochrome b562. Protein Sci 1998 Apr;7(4):961-5.
- Pfeil W. Thermodynamics of apocytochrome b5 unfolding. Protein Sci 1993 Sep;2(9):1497-501.
- Barker PD, Ferrer JC, Mylrajan M, Loehr TM, Feng R, Konishi Y, Funk WD, MacGillivray RT, Mauk AG. Transmutation of a heme protein. Proc Natl Acad Sci U S A 1993 Jul 15;90(14):6542-6.
- De Sanctis G, Ascoli F, Brunori M. Folding of apominimyoglobin. Proc Natl Acad Sci U S A 1994 Nov 22;91(24):11507-11.
- Zhong M, Lin L, Kallenbach NR. A method for probing the topography and interactions of proteins: footprinting of myoglobin. Proc Natl Acad Sci U S A 1995 Mar 14;92(6):2111-5.
- Zehfus MH. Automatic recognition of hydrophobic clusters and their correlation with protein folding units. Protein Sci 1995 Jun;4(6):1188-202.
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