Spectrometric-based techniques for metal-binding protein assessment in clinical, environmental, and food samples. Issue 2 (7th February 2017)
- Record Type:
- Journal Article
- Title:
- Spectrometric-based techniques for metal-binding protein assessment in clinical, environmental, and food samples. Issue 2 (7th February 2017)
- Main Title:
- Spectrometric-based techniques for metal-binding protein assessment in clinical, environmental, and food samples
- Authors:
- Chantada-Vázquez, María Pilar
Moreda-Piñeiro, Antonio
Barciela-Alonso, María Carmen
Bermejo-Barrera, Pilar - Abstract:
- ABSTRACT: Metalloproteins and metal–protein complexes play key roles in all organisms. For example, certain metalloproteins are involved in metal homeostasis and detoxification, or oxidative stress protection; whereas, metals serve as essential cofactors in a large number of metal–protein complexes. Advances in analytical instrumentation as well as informatics have allowed a complete characterization/assessment of both metalloproteins and metal–protein complexes. In some cases, the identification of the protein is a key factor for understanding its physiological function, such as when assessing protein corona in nanoparticles–protein assemblies. On other occasions, the identification of the binding sites in the peptide chain and conformational changes as a consequence of the metal–protein interaction, as well as the lability of this interaction, can explain the role of these metal-based biomolecules in living organisms. This article attempts to critically review the current state-of-the-art of the available analytical techniques for characterizing metalloproteins and metal–protein complexes. Methods for assessing the structure, characterization of the metal-binding sites, as well as the class of proteins involved in some metal (metallic nanoparticle)-binding proteins are discussed. Recent developments when assessing metalloproteins and metal–protein complexes in the clinical, environmental, and food fields, and pioneering research regarding nanoparticle–proteinABSTRACT: Metalloproteins and metal–protein complexes play key roles in all organisms. For example, certain metalloproteins are involved in metal homeostasis and detoxification, or oxidative stress protection; whereas, metals serve as essential cofactors in a large number of metal–protein complexes. Advances in analytical instrumentation as well as informatics have allowed a complete characterization/assessment of both metalloproteins and metal–protein complexes. In some cases, the identification of the protein is a key factor for understanding its physiological function, such as when assessing protein corona in nanoparticles–protein assemblies. On other occasions, the identification of the binding sites in the peptide chain and conformational changes as a consequence of the metal–protein interaction, as well as the lability of this interaction, can explain the role of these metal-based biomolecules in living organisms. This article attempts to critically review the current state-of-the-art of the available analytical techniques for characterizing metalloproteins and metal–protein complexes. Methods for assessing the structure, characterization of the metal-binding sites, as well as the class of proteins involved in some metal (metallic nanoparticle)-binding proteins are discussed. Recent developments when assessing metalloproteins and metal–protein complexes in the clinical, environmental, and food fields, and pioneering research regarding nanoparticle–protein characterization, are also reviewed. … (more)
- Is Part Of:
- Applied spectroscopy reviews. Volume 52:Issue 2(2017)
- Journal:
- Applied spectroscopy reviews
- Issue:
- Volume 52:Issue 2(2017)
- Issue Display:
- Volume 52, Issue 2 (2017)
- Year:
- 2017
- Volume:
- 52
- Issue:
- 2
- Issue Sort Value:
- 2017-0052-0002-0000
- Page Start:
- 145
- Page End:
- 174
- Publication Date:
- 2017-02-07
- Subjects:
- Analytical -- atomic -- biological -- ICP-MS -- mass spectrometry -- molecular
Spectrum analysis -- Periodicals
535.84 - Journal URLs:
- http://www.tandfonline.com/ ↗
- DOI:
- 10.1080/05704928.2016.1213736 ↗
- Languages:
- English
- ISSNs:
- 0570-4928
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 1579.500000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 581.xml