BBA Report
Biological membranes are rich in low-frequency motion

https://doi.org/10.1016/0005-2736(83)90065-2Get rights and content

Abstract

Using 13C cross-polarization NMR techniques, we have found that the effect of protein on the dynamics of the hydrocarbon interior of a series of biological membranes is to depress the intensity of motion on the nanosecond timescale (i.e., T1 becomes longer) and to enhance the intensity of motion on the timescale of tens of microseconds (i.e., T1p becomes shorter).

References (36)

  • P.J. Quinn

    Prog. Biophys. Mol. Biol.

    (1981)
  • H.C. Jarrell et al.

    Biochim. Biophys. Acta

    (1982)
  • S. Fleischer et al.

    Biophys. J.

    (1982)
  • B.A. Cornell et al.

    Biochim. Biophys. Acta

    (1982)
  • R. Smith

    Biochim. Biophys. Acta

    (1977)
  • J.M. Anderson et al.

    Biochim. Biophys. Acta

    (1966)
  • K. Leto et al.

    Biochim. Biophys. Acta

    (1981)
  • D. Oesterhelt et al.

    Methods Enzymol.

    (1974)
  • G.B. Ralston

    Biochim. Biophys. Acta

    (1976)
  • I.J. Ryrie et al.

    Arch. Biochem. Biophys.

    (1979)
  • D. Oesterhelt et al.

    FEBS Lett.

    (1974)
  • A. Hara et al.

    Anal. Biochem.

    (1978)
  • D.A. Torchia

    J. Magn. Reson.

    (1978)
  • T.H. Haines

    Biophys. J.

    (1982)
  • A. Cooper

    Sci. Prog.

    (1980)
  • D.E. Weiss

    Sub-Cell. Biochem.

    (1973)
  • J. Seelig et al.

    Q. Rev. Biophys.

    (1980)
  • R.E. Jacobs et al.

    Prog. Nucl. Magn. Reson. Spectrosc.

    (1981)
  • Cited by (0)

    View full text