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Study on the conformation of insulin by solvent perturbation and ultraviolet spectroscopy
Abstract
This study attempted to gain an insight of the conformation of insulin using solvent perturbation and ultraviolet spectroscopy. The effects of two solvents, mercaptoethanol and sucrose on the absorption spectrum of Insulin were studied; changes in ionic strength and pH were used to identify the position of amino acid chromophores. The effect on the absorption spectrum of movement from a non-polar to a polar environment indicates that tyrosine and phenylalanine reside on the surface of insulin protein. The results show that pH resolved spectral behavior of Insulin in the neighborhood of 290 nm is determined predominantly by the ionization of imidazole – NH+ of histidine. The results, however, do not rule out the possible contribution of the phenol hydroxyl of tyrosine in the spectral behavior. © 2013 International Formulae Group. All rights reserved.
Keywords: Insulin conformation, solvent perturbation, ultraviolet spectroscopy.
