Raman, Infrared, and Circular Dichroism Spectroscopic Studies on Metallothionein: A Predominantly “Turn”-Containing Protein

J. Pande, C. Pande, R. Callender, J. Pande, D. Gilg, M. Vašák, J. H.R. Kägi

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Abstract

Raman and IR spectra of rabbit liver metallothionein 1 (MT-1) containing 7 mol of either cadmium or zinc ions reveal high-lying amide III bands between 1290 and 1330 cm-1, indicative of 0-turns. A comparison of the splitting pattern in the amide III region below 1290 cm-1 and in the amide I band between 1600 and 1700 cm-1, with the normal-mode calculations of Lagant et al. [Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984 a) Eur. J. Biochem. 139, 137-148; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984 b) Eur. J. Biochem. 139, 149-154; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984 c) J. Raman Spectrosc. 15, 421–423] and Krimm and Bandekar [Krimm, S., & Bandekar, J. (1980) Biopolymers 19, 1–29], suggests that metal-bound (holo) MT-1 consists largely of β-turns of type II. In contrast, the metal-free (apo) protein displays a predominantly unordered conformation. The Raman spectra of the holoproteins below 1000 cm-1 are characterized by several unusual skeletal stretching and bending modes. The spectral pattern between 760 and 800 cm-1 in conjunction with the splitting of the amide I band agrees closely with the normal-mode calculations of Lagant et al. (1984 b) on model peptides and is indicative of the presence of type III β-turns (or 310-helical segments) in MT-1. The good agreement between the vibrational spectroscopic results presented here on MT-1 and the 2D NMR solution structure and X-ray crystal structure data on MT-2 [Braun, G., Wagner, G., Wörgötter, E., Vašák, M., Kägi, J. H. R., & Wüthrich, K. (1986) J. Mol. Biol. 187, 125-129; Wagner, G., Neuhaus, D., Wörgötter,. E., Vašák, M., Kagi, J. H. R., & Wüthrich, K. (1986) J. Mol. Biol. 187, 131-135; Furey, W. F., Robbins, A. H., Clancy, L. L., Winge, D. R., Wang, B. C., & Stout, C. D. (1986) Science (Washington, D.C.) 231, 704–710] demonstrates that both isoforms of the protein assume nearly identical folding patterns.

Original languageEnglish (US)
Pages (from-to)5526-5532
Number of pages7
JournalBiochemistry
Volume25
Issue number19
DOIs
StatePublished - Sep 1986

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ASJC Scopus subject areas

  • Biochemistry

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