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Infrared spectra in 2H2O solution of guanylic acid helices and of poly-G

✍ Scribed by H.Todd Miles; Joe Frazier


Publisher
Elsevier Science
Year
1964
Weight
203 KB
Volume
79
Category
Article
ISSN
0926-6577

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✦ Synopsis


the tyrosine and tryptophan residues. Whether such changes are a sufficient condition for the occurrence of the low-wavelength difference peak is uncertain since the possibility can be considered that contributions from other chromophores, e.g., the peptide bond, may occur simultaneously with the spectral changes at the higher-wavelength region. It is worthy of note, however, that EISENBERG AND EDSALL v have recently determined that the ratio of the difference peak at 236 to that at 287 m~ remained constant upon exposure of human serum albumin to a variety of denaturation conditions. They thus concluded that the low-wavelength peak for this protein has its origins in the surroundings of the tyrosine residues and that "contributions from other groups, or from changes in the conformation of the peptide chain, would appear to play a negligible role insofar as the difference spectrum is concerned".

The possible relation of the difference absorbancy peak at approx. 230 m/~ to conformational changes of other proteins is currently being investigated in this laboratory and will be reported in detail at a later date.


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