About this Biochemistry, Genetics and Molecular Biology article

Static and dynamic quenching of protein fluorescence. II. Lysozyme by Robert McGuire; Isaac Feldman is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

## Abstract The fluorescence parameters—lifetime, relative quantum yield, wavelength of maximum fluorescence intensity, half‐width, and polarization—of 0.01% lysozyme were measured at 15°C in aqueous solution, in glycerol–water mixtures (0–90% v/v glycerol), in aqueous urea (0–8__M__) solutions, and in aqueous guanidine hydrochloride (0–6.4__M__) solutions. The changes in the static and dynamic quenching of lysozyme fluorescence, monitored by the quantum yield and lifetime measurements, were correlated with the other fluorescence parameters and compared with our earlier results with bovine serum albumin. The results were interpreted in terms of induced conformational changes. The various perturbants altered the fluorescence parameters of lysozyme and bovine serum albumin very differently. The differences were shown to be entirely consistent with our earlier conclusion that bovine serum albumin fluorophores are nonsurface residues and with the conclusion of others that lysozyme fluorophores are surface residues. Unlike their effects on bovine serum albumin, urea and guanidine hydrochloride affect lysozyme structure quite differently, both in nature and degree. We have suggested that

Author

Robert McGuire; Isaac Feldman

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

1975

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)