The raman spectrum of biosynthetic human growth hormone. Its deconvolution,bandfitting, and interpretation |
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| Institution: | 1. Lilly Research Laboratories, Lilly Corporate Center, Indianapolis, IN 46285 U.S.A.;1. Department of Physics, Arignar Anna Govt.Arts College, Cheyyar 604407, Tamilnadu, India;2. Thiruvalluvar University, Serkadu, Vellore 632115, Tamilnadu, India;3. Department of Physics, Puratchi Thalaivar Dr.M.G.R. Govt. Arts and Science College, Uthiramerur 603406, India;4. Department of Chemistry, College of Science, King Khalid University, P.O. Box 9004, Abha 61413, Saudi Arabia;5. Research Center for Advanced Materials Science (RCAMS), King Khalid University, P.O. Box 9004, Abha 61413, Saudi Arabia;1. University of Potsdam, Institute of Chemistry, Physical Chemistry – innoFSPEC, Am Mühlenberg 3, 14476 Potsdam, Germany;2. University of Potsdam, Institute of Chemistry, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany;1. Institute of Hydrology and Water Resources, Civil Engineering, Zhejiang University, Hangzhou 310058, China;2. Institute of Applied Remote Sensing and Information Technology, Zhejiang University, Hangzhou 310058, China;1. Bio-Inspired Surface Engineering and Biomineralization Lab, Department of Materials Science and Engineering, Technion – Israel Institute of Technology, 32000, Haifa, Israel;2. Laboratory of Pharmaceutical Nanomaterials Science, Department of Materials Science and Engineering, Technion – Israel Institute of Technology, 32000, Haifa, Israel;1. College of Natural Resources and Environment, Northwest A&F University, Yangling, Shaanxi 712100, China;2. Research Center of Recycle Agricultural Engineering and Technology of Shaanxi Province, Northwest A&F University, Yangling, Shaanxi 712100, China |
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| Abstract: | The Raman spectrum of amorphous biosynthetic human growth hormone, somatotropin, has been measured at high signal-to-noise ratios, using a CW argon ion laser and single channel detection. The rms signal-to-noise ratio varies from 1800:1 in the Amide I region near 1650 cm−1 region, to 500:1 in the disulfide stretch region near 500 cm−1.Component Raman bands have been extracted from the entire spectral envelope from 1800-400 cm−1, by an interactive process involving both partial deconvolution and band-fitting. Interconsistency of all bands has been achieved by multiple overlapping of adjacent regions that had been isolated for the band-fitting programs.The resulting areas of the Raman component bands have been interpreted to show the ratios of peptide conformations in the hormone: 64% α-helix, 24% β-sheet, 8% β-turns and 4% γ-turns. Analysis of the tyrosine region, usually described as a Fermi resonance doublet near ∼830–850 cm−1, shows four bands, at 825, 833, 853, and 859 cm−1 in this macromolecule. Integrated intensities of these bands (2:2:2:2) are interpreted to show that only half of the eight tyrosine residues function as hydrogen-bond bridges via the acceptance of protons.Both disulfide bridges fall within the frequency ranges for normal, unstressed SS bonds: The 511 and 529 cm−1 bands are indicative of the gauche-gauche-gauche and trans-gauche-gauche conformations, respectively. |
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