Vw. Couling et al., ULTRAVIOLET RESONANCE RAMAN-SPECTROSCOPIC STUDY OF THE AVERAGE ENVIRONMENT OF TYROSINE IN NATIVE AND DENATURED BARNASE, Journal of Raman spectroscopy, 28(1), 1997, pp. 33-38
Ultraviolet resonance Raman spectroscopy was used to probe the change
in the average environment of the seven tyrosine amino acids in barnas
e when the polypeptide chain folds from the denatured to the native st
ate, The excitation radiation was continuous wave at a wavelength of 2
44 nm, and was generated from an intracavity-doubled argon ion laser,
a BBO non-linear optical crystal being placed within the laser cavity.
The change in the intensity ratio of the tyrosine Fermi-resonance dou
blet at 830/850 cm(-1) was calibrated to provide a spectroscopic indic
ator of tyrosine hydrogen-bond strength. This was achieved by using p-
cresol as a model compound, and measuring the resonance Raman spectra
of p-cresol when dissolved in a range of solvents with known hydrogen-
bond enthalpies of formation. (C) 1997 by John Wiley & Sons, Ltd.