Influence of Cations on Secondary Structures of Macromolecules and Membranes - IR Investigations

  • Georg Zundel
Conference paper
Part of the The Jerusalem Symposia on Quantum Chemistry and Biochemistry book series (JSQC, volume 8)

Abstract

In the IR spectra coupling of vibrations leads to band splitting and bands shifting in opposite directions, thus providing information on the orientation of groupings of macromolecules relative to each other. — With polynucleotides base pairing is indicated by such coupling effects with the C=O stretching vibrations. — With ribo(polynucleotides) coupling of the 2’OD bending vibration with the C—O—C stretching vibration of the ether group of ribose residues proves that the ribose residues may be cross-linked via hydrogen bonds, which are formed by the 2’OD groups with the ether O atom of neighboring ribose residues. These H-bonds stiffen the backbone of RNA, inducing, for instance with homoribo (polynucleotides) in neutral medium, rod-like structures. The influence of cations is discussed. Two conformations of the backbone are observed: (a) The Open image in new window groups can be turned outward at the backbone. (b) The Open image in new window groups can be turned toward the base residues. The latter may be induced by cations with strong fields. - It is shown that the conformation of Mg2+ poly(U) is probably a triple and not a double helix. - Melting of base pairing and backbone structure of t·RNA Phe with temperature and dialysis against distilled water are discussed. It is shown that Mg2+ ions increase the melting temperature by 40°C. This effect is preferentially caused by a change of the tertiary and not the secondary structure. In contrast to this result, with 23 S RNA the double helical regions become more compact and strong hydrogen bonds are formed between the 2’OH groups and the ether O atom of neighboring ribose residues, which is due to the influence of Mg2+ ions.

Finally, vesicles from excitable membranes are investigated. It is shown that in the presence of K+ ions the conformation of relatively large parts of the membrane proteins occur as an antiparallel β-structure, whereas in the presence of Na+ and Ca2+ ions the proteins are largely helical. Thus it seems highly probable that during the action potential membrane proteins change their conformation, depending on the cations present in the membrane.

Keywords

Secondary Structure Cacodylate Buffer Double Helix Triple Helix Base Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© D. Reidel Publishing Company, Dordrecht-Holland 1976

Authors and Affiliations

  • Georg Zundel
    • 1
  1. 1.Institute of Physical ChemistryUniversity of MunichMünchen 2West Germany

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