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- W286113241 abstract "The chapter focuses on modification of the secondary structure of hemoprotein molecules. Any modification of the secondary structure of protein molecules will cause diverse alterations of their essential properties. The chapter presents the studies that were made on the hemochrome-forming chemical groups of some hemoproteins after the proteins had been artificially unfolded. The heme–heme interaction, the Bohr Effect, and the affinity for ethyl isocyanide of hemoglobin were independent of each other and were affected in different ways by urea. The addition of various carboxylic acid salts and detergents to hemoglobin and cytochrome c caused modification of the secondary protein structure and alteration of the proper functioning of the hemoproteins. The affinity of basic amino acids for heme appeared to increase when the acids were integrated into larger peptide molecules. These studies highlight the importance of the secondary structure of the protein moieties of hemoproteins for their specific functions." @default.
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- W286113241 date "1961-01-01" @default.
- W286113241 modified "2023-09-24" @default.
- W286113241 title "MODIFICATION OF THE SECONDARY STRUCTURE OF HAEMOPROTEIN MOLECULES" @default.
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- W286113241 doi "https://doi.org/10.1016/b978-1-4831-9646-6.50013-2" @default.
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