Raman, infrared, and circular dichroism spectroscopic studies on metallothionein

A predominantly "turn"-containing protein

J. Pande, C. Pande, Robert Callender, M. Vašák, R. Callender, J. H R Kägi

Research output: Contribution to journalArticle

38 Citations (Scopus)

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 β-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. (1984a) Eur. J. Biochem. 139, 137-148; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984b) Eur. J. Biochem. 139, 149-154; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984c) 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. (1984b) 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., Kägi, 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
StatePublished - 1986
Externally publishedYes

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Metallothionein
Circular Dichroism
Amides
Infrared radiation
Proteins
Metals
Biopolymers
Cadmium
Liver
Stretching
Conformations
Raman scattering
Zinc
Protein Isoforms
Crystal structure
Nuclear magnetic resonance
X-Rays
Ions
Rabbits
X rays

ASJC Scopus subject areas

  • Biochemistry

Cite this

Raman, infrared, and circular dichroism spectroscopic studies on metallothionein : A predominantly "turn"-containing protein. / Pande, J.; Pande, C.; Callender, Robert; Vašák, M.; Callender, R.; Kägi, J. H R.

In: Biochemistry, Vol. 25, No. 19, 1986, p. 5526-5532.

Research output: Contribution to journalArticle

Pande, J, Pande, C, Callender, R, Vašák, M, Callender, R & Kägi, JHR 1986, 'Raman, infrared, and circular dichroism spectroscopic studies on metallothionein: A predominantly "turn"-containing protein', Biochemistry, vol. 25, no. 19, pp. 5526-5532.
Pande, J. ; Pande, C. ; Callender, Robert ; Vašák, M. ; Callender, R. ; Kägi, J. H R. / Raman, infrared, and circular dichroism spectroscopic studies on metallothionein : A predominantly "turn"-containing protein. In: Biochemistry. 1986 ; Vol. 25, No. 19. pp. 5526-5532.
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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 β-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. (1984a) Eur. J. Biochem. 139, 137-148; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984b) Eur. J. Biochem. 139, 149-154; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984c) 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. (1984b) 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., W{\"o}rg{\"o}tter, E., Vaš{\'a}k, M., K{\"a}gi, J. H. R., & W{\"u}thrich, K. (1986) J. Mol. Biol. 187, 125-129; Wagner, G., Neuhaus, D., W{\"o}rg{\"o}tter, E., Vaš{\'a}k, M., K{\"a}gi, J. H. R., & W{\"u}thrich, 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.",
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T2 - A predominantly "turn"-containing protein

AU - Pande, J.

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AU - Callender, Robert

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AU - Callender, R.

AU - Kägi, J. H R

PY - 1986

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N2 - 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 β-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. (1984a) Eur. J. Biochem. 139, 137-148; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984b) Eur. J. Biochem. 139, 149-154; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984c) 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. (1984b) 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., Kägi, 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.

AB - 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 β-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. (1984a) Eur. J. Biochem. 139, 137-148; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984b) Eur. J. Biochem. 139, 149-154; Lagant, P., Vergoten, G., Fleury, G., & Loucheux-Lefebvre, M. (1984c) 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. (1984b) 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., Kägi, 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.

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