A method to probe protein structure from UV absorbance spectra.
Anal Biochem
; 587: 113450, 2019 12 15.
Article
em En
| MEDLINE
| ID: mdl-31550438
ABSTRACT
Proteins primarily absorb UV light due to the presence of tryptophan, tyrosine, and phenylalanine residues, with absorbance maxima at 280, 275, and 258 nm, respectively. We now demonstrate that a simple value obtained by relating the absorbance at all three wavelengths, [A280/A275 + A280/A258], is a generally useful, robust, and sensitive probe of protein 'foldedness', and thus can be used to investigate unfolding, refolding, disulfide bonds, stability, buffer excipients, and even protein-protein and protein-ligand interactions.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Raios Ultravioleta
/
Pepsina A
/
Ácido Aspártico Proteases
Idioma:
En
Revista:
Anal Biochem
Ano de publicação:
2019
Tipo de documento:
Article