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. 1983 Dec 1;215(3):465–469. doi: 10.1042/bj2150465

Identification of low-frequency modes in protein molecules.

K C Chou
PMCID: PMC1152424  PMID: 6362659

Abstract

It is demonstrated that the observed low-frequency motions with wave numbers of 22 cm-1 and 25 cm-1 for insulin and lysozyme respectively originate from the accordion-like motions of the principal helices therein. The calculated results based on such a model are in good agreement with the observed values. During calculations the role of the internal microenvironment upon the low-frequency motion is naturally revealed, so as to elucidate as well why this kind of low-frequency motion is so sensitive to the conformations of proteins observed.

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Selected References

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  1. Blake C. C., Koenig D. F., Mair G. A., North A. C., Phillips D. C., Sarma V. R. Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution. Nature. 1965 May 22;206(4986):757–761. doi: 10.1038/206757a0. [DOI] [PubMed] [Google Scholar]
  2. Brown K. G., Erfurth S. C., Small E. W., Peticolas W. L. Conformationally dependent low-frequency motions of proteins by laser Raman spectroscopy. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1467–1469. doi: 10.1073/pnas.69.6.1467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Careri G., Fasella P., Gratton E. Statistical time events in enzymes: a physical assessment. CRC Crit Rev Biochem. 1975 Aug;3(2):141–164. doi: 10.3109/10409237509102555. [DOI] [PubMed] [Google Scholar]
  4. Fanconi B., Small E. W., Peticolas W. L. Phonon dispersion curves and normal coordinate analysis of -poly-L-alanine. Biopolymers. 1971;10(8):1277–1298. doi: 10.1002/bip.360100804. [DOI] [PubMed] [Google Scholar]
  5. Genzel L., Keilmann F., Martin T. P., Winterling G., Yacoby Y., Fröhlich H., Makinen M. W. Low-frequency Raman spectra of lysozyme. Biopolymers. 1976 Jan;15(1):219–225. doi: 10.1002/bip.1976.360150115. [DOI] [PubMed] [Google Scholar]
  6. Ito K., Shimanouchi T. Vibrational frequencies and modes of alpha-helix. Biopolymers. 1970;9(4):383–399. doi: 10.1002/bip.1970.360090402. [DOI] [PubMed] [Google Scholar]
  7. Ji S. Energy and negentropy in enzymic catalysis. Ann N Y Acad Sci. 1974 Feb 18;227:419–437. doi: 10.1111/j.1749-6632.1974.tb14405.x. [DOI] [PubMed] [Google Scholar]
  8. Painter P. C., Mosher L. E., Rhoads C. Low-frequency modes in the Raman spectra of proteins. Biopolymers. 1982 Jul;21(7):1469–1472. doi: 10.1002/bip.360210715. [DOI] [PubMed] [Google Scholar]
  9. Richardson J. S. The anatomy and taxonomy of protein structure. Adv Protein Chem. 1981;34:167–339. doi: 10.1016/s0065-3233(08)60520-3. [DOI] [PubMed] [Google Scholar]
  10. Sobell H. M., Lozansky E. D., Lessen M. Structural and energetic considerations of wave propagation in DNA. Cold Spring Harb Symp Quant Biol. 1979;43(Pt 1):11–19. doi: 10.1101/sqb.1979.043.01.004. [DOI] [PubMed] [Google Scholar]
  11. Suezaki Y., Go N. Breathing mode of conformational fluctuations in globular proteins. Int J Pept Protein Res. 1975;7(4):333–334. doi: 10.1111/j.1399-3011.1975.tb02448.x. [DOI] [PubMed] [Google Scholar]

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