2016
DOI: 10.1007/s12551-016-0198-6
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UV–Vis spectroscopy of tyrosine side-groups in studies of protein structure. Part 1: basic principles and properties of tyrosine chromophore

Abstract: Spectroscopic properties of tyrosine residues may be employed in structural studies of proteins. Here we discuss several different types of UV–Vis spectroscopy, like normal, difference and second-derivative UV absorption spectroscopy, fluorescence spectroscopy, linear and circular dichroism spectroscopy, and Raman spectroscopy, and corresponding optical properties of the tyrosine chromophore, phenol, which are used to study protein structure.

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Cited by 62 publications
(49 citation statements)
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“…Chromophores have characteristic absorbance bands. Changing their environment either by adding another compound or altering the physical environment, like raising temperature, may change their energy levels and thus the wavelength and the intensity of absorbance . Band shifts to longer wavelengths (red‐shift) are bathochromic shifts and shifts to shorter wavelengths (blue‐shift) are hypsochromic shifts.…”
Section: Introductionmentioning
confidence: 99%
“…Chromophores have characteristic absorbance bands. Changing their environment either by adding another compound or altering the physical environment, like raising temperature, may change their energy levels and thus the wavelength and the intensity of absorbance . Band shifts to longer wavelengths (red‐shift) are bathochromic shifts and shifts to shorter wavelengths (blue‐shift) are hypsochromic shifts.…”
Section: Introductionmentioning
confidence: 99%
“…For HPA [Figure (A‐1)], there are two main peaks at 224 and 276 nm from the ππ transition. The first transition is from ππ transition of the phenyl ring while the second transition is from nπ of carbonyl group in monomer structure . After polymerization, both monomer peaks exhibited a red shift by 5–10 nm with longer tail absorption to 450 nm.…”
Section: Resultsmentioning
confidence: 99%
“…p à of carbonyl group in monomer structure. 45 After polymerization, both monomer peaks exhibited a red shift by 5-10 nm with longer tail absorption to 450 nm. This red shift is from electron delocalization due to higher conjugated length, and formation of polymer with lower energy required for the p !…”
Section: Uv-vis Analysis Of Polyphenolsmentioning
confidence: 98%
“…Tyrosine exhibits fingerprint peaks at 280 and 230 nm due to phenol and carboxylic acid, respectively. [ 22 ] Alanine (A), an amino acid, exhibits a broad peak from 200 to 240 nm, [ 23 ] and cysteine (C), an amino acid, has a weak peak at 260 nm due to disulfide bonding. [ 24 ] The absorbance of pristine peptide film exhibits three prominent peaks at 200, 230, and 280 nm, which mainly originate from the π to π* transition in the peptide bond, [ 24 ] from the carboxylic acid in tyrosine, and from the phenol in tyrosine, respectively.…”
Section: Figurementioning
confidence: 99%