2013
DOI: 10.1016/j.cplett.2012.12.050
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Terahertz time-domain and FTIR spectroscopic study of interaction of α-chymotrypsin and protonated tris with 18-crown-6

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Cited by 12 publications
(3 citation statements)
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“…It is rather common to perform ultra-broadband spectroscopic measurements combining FTIR with TPS, which typically covers a range from 0.1 to 4.5THz [166][167][168]. However, TPS is often applied without FTIR, since it provides important broadband spectral information.…”
Section: Instruments Of Terahertz Spectroscopy and Imaging For Tissue...mentioning
confidence: 99%
“…It is rather common to perform ultra-broadband spectroscopic measurements combining FTIR with TPS, which typically covers a range from 0.1 to 4.5THz [166][167][168]. However, TPS is often applied without FTIR, since it provides important broadband spectral information.…”
Section: Instruments Of Terahertz Spectroscopy and Imaging For Tissue...mentioning
confidence: 99%
“…The emergence of THz‐TDS stimulated a lot of interest to investigate the properties of a wide range of materials but it was not until 2000 when the first work was published on the use of THz‐TDS to study proteins . Since then, THz‐TDS has been used to study a range of protein structures and dynamics which showed promise for smaller peptides, proteins and large macromolecular complexes . What hindered analysis of proteins using THz‐TDS was the strong absorption at terahertz frequencies of the highly abundant water compared with the small quantities of protein.…”
Section: Introductionmentioning
confidence: 99%
“…[1][2][3] The presence of crown-ether molecules in organic solvents leads to an increase in the activity by several orders of magnitude due to the interaction with surface amino groups. The structure of the surface amino acid residues can easily be changed using variations in the native (aqueous) environment of a protein molecule.…”
Section: Introductionmentioning
confidence: 99%