Identification of low-frequency modes in protein molecules
- 1 December 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 215 (3) , 465-469
- https://doi.org/10.1042/bj2150465
Abstract
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 on 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 conformation of proteins observed.This publication has 14 references indexed in Scilit:
- The Anatomy and Taxonomy of Protein StructurePublished by Elsevier ,1981
- Structural and Energetic Considerations of Wave Propagation in DNACold Spring Harbor Symposia on Quantitative Biology, 1979
- Low‐frequency Raman spectra of lysozymeBiopolymers, 1976
- BREATHING MODE OF CONFORMATIONAL FLUCTUATIONS IN GLOBULAR PROTEINSInternational Journal of Peptide and Protein Research, 1975
- Statistical Time Events in Enzymes: A Physical AssessmenCRC Critical Reviews in Biochemistry, 1975
- ENERGY AND NEGENTROPY IN ENZYMIC CATALYSIS*Annals of the New York Academy of Sciences, 1974
- Conformationally Dependent Low-Frequency Motions of Proteins by Laser Raman SpectroscopyProceedings of the National Academy of Sciences, 1972
- Phonon dispersion curves and normal coordinate analysis of α‐poly‐L‐alanineBiopolymers, 1971
- Vibrational frequencies and modes of α‐helixBiopolymers, 1970
- Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å ResolutionNature, 1965