Abstract
Bacterial cells, because of their relatively simple organization, have proved to be useful model systems for studying how the structure and function of cellular organelles are determined by the course of their biosynthesis. Although the sequence of the biochemical events leading to the assembly of cellular structural components determine to a large extent function and supramolecular structure, the physicochemical properties of the biopolymers themselves might also contribute to shape and function (1). Less is known about the in vivo physicochemical properties of biopolymers, than about their biosynthesis. An understanding of the three-dimensional structures and molecular dynamics of biopolymers is often required to bridge the gap between biochemical information on the one hand, and the structure of a cellular organelle, as revealed by electron microscopy, on the other. An example is the expression of the morphogenetically determined shapes of bacteria. The shape of a bacterial cell is maintained by the rigid peptidoglycan layer in its cell wall (2). It was once believed that correlations could be made between the shapes of bacteria and the chemical composition of the peptidoglycan layer (2).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
H.J. Rogers (1974) Ann.N.Y.Acad.Sci. 235:29–51.
W. Weidel and H. Pelzer (1964) Adv.Enzymol. 26:193–232.
H.J. Rogers, M. McConnell and R.C. Hughes (1971) Journal of General Microbiology 66:297–308.
U. Schwartz and W. Leutgeb (1971) J.Bacterid. 106:588–595.
J. Schaefer (1974) in: G.C. Levy (ed), Topics in Carbon-13 NMR Spectroscopy, John Wiley & Sons, New York, pp.150–208.
F. Heatley and A. Begum (1976) Polymer: 399–408.
J. Schaefer, E.O. Stejskal and R. Buchdahl (1977) Macromolecules 10:384–405.
N.J.M. Birdsall, D.J. Ellar, A.G. Lee, J.C. Metcalfe and G.B. Warren (1975) Biochim.Biophys.Acta 380:344–354.
A. Daniels, R.J.P. Williams and P.E. Wright (1976) Nature 261:321–323.
R.T. Eakin, L.O. Mórgan, C.T. Gregg and N.A. Matwiyoff (1972) FEBS Letters 28:259–264.
D. Gust, R.B. Moon and J.D. Roberts (1975) Proc.Natl.Acad.Sci.USA 72:4696–4700.
G.E. Hawkes, E.W. Randall and C.H. Bradley (1976) Nature 257:767–772.
V. Markowski, T. Posner, P. Loftus and J.D. Roberts (1977) Proc.Natl.Acad.Sci.USA 94:1308–1309.
M. Llinas and K.Würthrich, Biochim.Biophys.Acta, in press.
F. Blomberg, W. Maurer and H. Rüterjans (1976) Proc.Natl.Acad. Sci.USA 73:1409–1413.
A. Lapidot, C.S. Irving and Z. Malik (1976) J.Am.Chem.Soc. 98:632–634.
A. Lapidot and C.S. Irving (1977) J.Am.Chem.Soc. 99:5488–5490.
C.S. Irving and A. Lapidot (1977) Biochim. Biophys.Acta 470:251–257.
A. Lapidot and C.S. Irving (1977) in: M. Goodman & J. Meienhofer (eds), Peptides, Proc.Fifth Amer.Peptide Symp. John Wiley & Sons, New York, pp.419–422.
M. Llinas, K. wüthrich, W. Schworzer and W. von Philipshorn (1975) Nature 257:817–818.
A. Lapidot and C.S. Irving (1977) Proc.Natl.Acad.Sci.USA 74:1988–1992.
G.R. Millward and D.A. Raveley (1974) J.Ultrastructure Res. 46:309–326.
R.E. Marquis (1968) J.Bacteriol. 95:776–781.
L.T. Ou and R.E. Marquis (1970) J.Bacteriol. 101:92–101.
L.T. Ou and R.E. Marquis (1972) Can.J.Microbiol. 18:623–629.
J.M. Ghuysen and C.D. Shockman (1973) in: Loretta Leive (ed), Bacterial Membranes and Walls, Marcel Dekker, Inc., New York, Chp.2.
J.M. Ghuysen (1968) Bact.Rev. 32:425.
E.M. Oldmixon, S. Glauser and M.L. Higgins (1974) Biopolymers 13:2037–2060.
J. Baddiley (1970) Accounts Chem.Res. 3:98–105.
R.C. Hughes, J.G. Pavlik, H.J. Rogers and P.J. Tanner (1968) Nature 219:642–644.
R. Scherrer and P. Gerhardt (1971) J.Bacteriol. 107:718–735.
R.E. Marquis, K. Mayzel and E.L. Carstensen (1976) Can.J.Microbiol. 22:975–982.
M.J. Tilby (1977) Nature 266:450–452.
N.H. Mendelson (1976) Proc.Natl.Acad.Sci.USA 44:1740–1744.
H.J. Rogers (1967) Nature 213:31–33.
J.M. Ghuysen (1972) Proc.Lysozyme Conf. pp. 185–193.
C.S. Irving and A. Lapidot (1975) J.Am.Chem.Soc. 97:5945–5946.
J.F. Farnell, E.W. Randall and A.I. White (1972) J.Chem.Soc.,Chem. Commun. 1159–1160.
E. Work (1971) in: J.R. Norris & D.W. Ribbons (eds), Methods in Microbiology, Academic Press, pp.361–418.
H.J. Rogers and C.W. Forsberg (1971) J.Bacteriol. 108:1235–1243.
M.V. Kelemen and H.J. Rogers (1971) Proc.Natl.Acad.Sci.USA 68:992–996.
R.C. Hughes and P.P. Thurman (1970) Biochem.J. 119:925–926.
J.T. Tipper (1970) International Journal of Systematic Bacteriology 20:361–377.
H. Formanek, S. Formanek and H. Wawra (1974) Eur.J.Biochem. 46, 279–294.
V. Braun, H. Gnirke, U. Henning and K. Renn (1973) J.Bacteriol. 114:1264–1270.
H.H.M. Balyuzi, D.A. Reaveley and R.E. Burge (1972) Nature New Biology 235, 252–253.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1978 D. Reidel Publishing Company, Dordrecht, Holland
About this paper
Cite this paper
Lapidot, A., Irving, C.S. (1978). An in vivo 15N NMR Study of Bacterial Cell Walls. In: Pullman, B. (eds) Nuclear Magnetic Resonance Spectroscopy in Molecular Biology. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 11. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-9882-7_33
Download citation
DOI: https://doi.org/10.1007/978-94-009-9882-7_33
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-009-9884-1
Online ISBN: 978-94-009-9882-7
eBook Packages: Springer Book Archive