Terahertz Spectroscopic Analysis in Protein Dynamics: Current Status

Proteins play a key role in living organisms. The study of proteins and their dynamics provides information about their functionality, catalysis and potential alterations towards pathological diseases. Several techniques are used for studying protein dynamics, e.g., magnetic resonance, fluorescence...

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Published inRadiation (Multidisciplinary Digital Publishing Institute) Vol. 2; no. 1; pp. 100 - 123
Main Authors Mancini, Tiziana, Mosetti, Rosanna, Marcelli, Augusto, Petrarca, Massimo, Lupi, Stefano, D’Arco, Annalisa
Format Journal Article
LanguageEnglish
Published Munich MDPI AG 07.02.2022
Subjects
Amino acids
Antibodies
Biological products
conformation
Coronaviruses
COVID-19
Crystallography
Gene expression
Immunoassay
Metabolism
Microscopy
Nitrogen
peptide
Proteins
Radiation
Severe acute respiratory syndrome coronavirus 2
terahertz
terahertz spectroscopy
X-rays
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Abstract Proteins play a key role in living organisms. The study of proteins and their dynamics provides information about their functionality, catalysis and potential alterations towards pathological diseases. Several techniques are used for studying protein dynamics, e.g., magnetic resonance, fluorescence imaging techniques, mid-infrared spectroscopy and biochemical assays. Spectroscopic analysis, based on the use of terahertz (THz) radiation with frequencies between 0.1 and 15 THz (3–500 cm−1), was underestimated by the biochemical community. In recent years, however, the potential of THz spectroscopy in the analysis of both simple structures, such as polypeptide molecules, and complex structures, such as protein complexes, has been demonstrated. The THz absorption spectrum provides some information on proteins: for small molecules the THz spectrum is dominated by individual modes related to the presence of hydrogen bonds. For peptides, the spectral information concerns their secondary structure, while for complex proteins such as globular proteins and viral glycoproteins, spectra also provide information on collective modes. In this short review, we discuss the results obtained by THz spectroscopy in the protein dynamics investigations. In particular, we will illustrate advantages and applications of THz spectroscopy, pointing out the complementary information it may provide.
AbstractList Simple SummaryProteins are large biomolecules carrying out several different indispensable activities in all living organisms. As their chemical composition and structure lead to specific functionalities, possible variations alter conformational transition and cause dysfunctions and pathological diseases. An emerging technique for their detection and characterization is THz spectroscopy. In this review, we illustrate its potentialities and drawbacks in protein study. We report the most remarkable experimental works of the last decades, constituting decisive steps for the scientific and technological progress in THz spectroscopy for biomolecules. The importance of information provided by THz spectroscopy is outlined, conforming it as powerful and useful technique for topical open questions, too.AbstractProteins play a key role in living organisms. The study of proteins and their dynamics provides information about their functionality, catalysis and potential alterations towards pathological diseases. Several techniques are used for studying protein dynamics, e.g., magnetic resonance, fluorescence imaging techniques, mid-infrared spectroscopy and biochemical assays. Spectroscopic analysis, based on the use of terahertz (THz) radiation with frequencies between 0.1 and 15 THz (3–500 cm−1), was underestimated by the biochemical community. In recent years, however, the potential of THz spectroscopy in the analysis of both simple structures, such as polypeptide molecules, and complex structures, such as protein complexes, has been demonstrated. The THz absorption spectrum provides some information on proteins: for small molecules the THz spectrum is dominated by individual modes related to the presence of hydrogen bonds. For peptides, the spectral information concerns their secondary structure, while for complex proteins such as globular proteins and viral glycoproteins, spectra also provide information on collective modes. In this short review, we discuss the results obtained by THz spectroscopy in the protein dynamics investigations. In particular, we will illustrate advantages and applications of THz spectroscopy, pointing out the complementary information it may provide.
Proteins play a key role in living organisms. The study of proteins and their dynamics provides information about their functionality, catalysis and potential alterations towards pathological diseases. Several techniques are used for studying protein dynamics, e.g., magnetic resonance, fluorescence imaging techniques, mid-infrared spectroscopy and biochemical assays. Spectroscopic analysis, based on the use of terahertz (THz) radiation with frequencies between 0.1 and 15 THz (3–500 cm−1), was underestimated by the biochemical community. In recent years, however, the potential of THz spectroscopy in the analysis of both simple structures, such as polypeptide molecules, and complex structures, such as protein complexes, has been demonstrated. The THz absorption spectrum provides some information on proteins: for small molecules the THz spectrum is dominated by individual modes related to the presence of hydrogen bonds. For peptides, the spectral information concerns their secondary structure, while for complex proteins such as globular proteins and viral glycoproteins, spectra also provide information on collective modes. In this short review, we discuss the results obtained by THz spectroscopy in the protein dynamics investigations. In particular, we will illustrate advantages and applications of THz spectroscopy, pointing out the complementary information it may provide.
Author Petrarca, Massimo
Lupi, Stefano
Marcelli, Augusto
Mancini, Tiziana
Mosetti, Rosanna
D’Arco, Annalisa
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  surname: Mosetti
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  givenname: Stefano
  surname: Lupi
  fullname: Lupi, Stefano
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  orcidid: 0000-0001-7990-5117
  surname: D’Arco
  fullname: D’Arco, Annalisa
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Snippet Proteins play a key role in living organisms. The study of proteins and their dynamics provides information about their functionality, catalysis and potential...
Simple SummaryProteins are large biomolecules carrying out several different indispensable activities in all living organisms. As their chemical composition...
SourceID doaj
proquest
crossref
SourceType Open Website
Aggregation Database
StartPage 100
SubjectTerms Amino acids
Antibodies
Biological products
conformation
Coronaviruses
COVID-19
Crystallography
Gene expression
Immunoassay
Metabolism
Microscopy
Nitrogen
peptide
Proteins
Radiation
Severe acute respiratory syndrome coronavirus 2
terahertz
terahertz spectroscopy
X-rays
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Title Terahertz Spectroscopic Analysis in Protein Dynamics: Current Status
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https://doaj.org/article/a55f2dba16cb475795242beb7edeece9
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