The Ultraviolet Absorption Spectra of Amino Acids and Phenol in Aqueous and Anhydrous Hydrogen Fluoride Solution
Chemistry, ultraviolet resolution, amino acids, anhydrous hydrogen fluoride
Chemistry | Physical Sciences and Mathematics
A knowledge of the structure of the protein molecule is very important to future work with proteins, whether it be for medical research or some other field. In approaching the problem, we have done preliminary work on amino acids by a study of their ultraviolet absorption spectra in anhydrous liquid hydrogen fluoride solution.
Results indicate that tyrosine and phenol are protonated by the strong acid, as evidenced by the hypsochromic shifts in the maxima. Tyrosine shifts from 275 to 269mn with a hypochromic shift from 1370 to 732 litres/mol.-cm. Phenol has a hypsochromic shift from 270 to 252mn and a hypochromic shift from 1450 to 80 litre/mol-cm. These effects have been interpreted in the light of modern resonance theory.
This work indicates that definite information on the structure of the amino acid molecule in HF solution is obtainable, thus making it worthwhile to do cryoscopic studies and subsequent work on proteins with this solvent.
Department 1 Awarding Honors Status
Chacko, C. J. (1956). The Ultraviolet Absorption Spectra of Amino Acids and Phenol in Aqueous and Anhydrous Hydrogen Fluoride Solution (Undergraduate honors thesis, University of Redlands). Retrieved from https://inspire.redlands.edu/cas_honors/273