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.
Highlights
Amino acids/proteins participate in the formation of cells and tissues, and they are responsible for life activities in living organisms, such as enzymes, antibodies, signaling and transporting molecules, cell membrane, metabolic or catalytic functions, etc. [1,2,3,4]
An important role of proteins is played in viral pathogenesis, where membrane proteins are generally responsible for infectious processes, anchoring the virus to human receptors, as happens for the SARS-CoV-2 coronavirus [5,6]
The interpretation of the results was entrusted by theoretical calculations based on Density Function Theory (DFT) [155,156]; the water molecule is recognized to locate the carboxyl group and the amino group of hydrated Lys molecule, while its vibrational modes are produced by a dihedral torsion or bond angle bend of molecular chains
Summary
Amino acids/proteins participate in the formation of cells and tissues, and they are responsible for life activities in living organisms, such as enzymes, antibodies, signaling and transporting molecules, cell membrane, metabolic or catalytic functions, etc. [1,2,3,4]. We review results obtained by THz spectroscopy and imaging in the study of amino acids and protein dynamics. The determination of total protein nitrogen is a pTrhoexmimoisttycotomoml foonr itmhemeuanrolyasasnaydsraarpeiednqzyumanet-ilfiinckateidonimomf uthneosporrobteenint acsosnatyesn,tl.ateTrhael fKlojewldiamhlm[u10n]oaasnsdayDaunmdasWmesettehrondbsloatrteinwg,idbeulyt outsheedr faonralnyutitcraitliotnechlanboelloinggiesan[1d6,q1u8a–l2i5ty] hcoanvetroblee[1n5a–d17o]p.tOedthienrbtieocmhneidqiucaelsaanrde uclsiendicaanl sdtupdreiefes.rrSeodmfeoranthaelyirtiaccaclumraecthy,oldoswfocrosmt oannidtgorreiantgaapnpdlicdaebtielicttyioinn amraenbyasfieedldosnwthheereabthileityidteontpifirocpataigoanteo/fapmroptleifiynsbiisomreoqlueicruedle,ssuinchcealsl cthueltubriceisnocrhoonninthice adceitde,ctbiiounreotfaansdpeLcoiwficryanmtiebtohdoyd.sHaoswweevlel ra,sthUeVsealbabsoorrpattoiorny.dHiaogwnoesvteicr, tpacimiflbacenrnneeoscoacded.twhsnhincanHydseToilaiomleqeophsydmtraufeyme,oemeetc,wpmhustfwptiiehlnoemorulseeedoenseonmqt.ariaabuscneuurrsroiseesairnbmceeeyotbiefdiomltnaamayimsscmfnosoeeederna-dreedcayWvocitniosmocanidneralmsdmulslutsteshaaeptumthynerreenneeidccaongcttbbagiorcmtvlioslgholiaesosinnettnacstyifiyodiscttanpisaptlocgousleyaane,scsrp,nbeiteopafruduoiorreocdtenpnsmtiiolieaezpmyttescgyirhv.tmhmeamaeeSfntrbueeeeoiroara/qn-merlslnuaeisieunecamuedrrlkseealeypt:eivsntsntdlpia.haXicfodllOeaiy-uymnrelttatabssothimtyecceitieorcaaouarihmllcnbnnnrmtoioedyotnorhcelsgsgleihettooatcahsntgrntulhobaiilqilqeoedceseusugknssnpar[etifinir1atssonaor6tp,rsoitc,cfhses1hgmieuaiy8ceanlyca–o,lnlhstl2ncdeni,p5uoiynault]rnlanosgetcht.urasilemaneEiemrrnvaengsaigers---,tl or on the detection of a specific antibody These laboratory diagnostic techniques require time to detect the specific immune response and its quantification. When used for virus recognition or metabolic evaluation the task is challenging, and some immunoassays may give false positive results Other techniques, such as microscopy, fluorescence and spectroscopy, are preferred in describing the protein dynamics. Only recently with the accessibility of ultrafast lasers, coherent Raman Scattering (CRS) techniques are going to assert themselves thanks to the sensitivity at the same molecular vibrations probed in spontaneous Raman spectroscopy and to the nonlinear dependence on the incoming light fields [30,31,32,33]
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