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- W2041986444 abstract "The far ultraviolet circular dichroism (CD) spectra of myoglobin, lysozyme, carboxypeptidase A, papain, and ribonuclease were compared with each other and with the spectra of several proteins of unknown conformation. The CD curve of carboxypeptidase A had negative peaks at 221 and 210 mμ and a positive peak at 193 mμ. Papain showed negative peaks at 222, 209 and 200 mμ, and a positive peak at 189–191 mμ. The CD spectra of human serum albumin, bacterial α-amylase, clostridiopeptidase A, enolase, hexokinase, hyaluronidase, lactate dehydrogenase, lipase, pyruvate kinase, and transferrin had negative peaks at 220–223 mμ and at 208–210 mμ and positive peaks at 190–193 mμ indicating significant amounts of the α-helix in these proteins. The CD spectra of Bence Jones proteins, cellulase, deoxyribonuclease, elastase, the immunoglobulin G immunoglobulins, pepsin and trypsin differed from each other and from those of the previously mentioned group. The interpretation of these spectra in terms of conformation is difficult, because the effects of the possible periodic orders are distorted by the effects of the side chain chromophores and by the aperiodic rigid structures of the polypeptide chain backbone." @default.
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- W2041986444 date "1970-01-01" @default.
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- W2041986444 title "Circular dichroism of proteins of known and unknown conformations" @default.
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- W2041986444 doi "https://doi.org/10.1016/0005-2795(70)90037-1" @default.
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