Biological membranes are rich in low-frequency motion

B. A. Cornell; R. G. Hiller; J. Raison; F. Separovic; R. Smith; J. C. Vary; C. Morris

doi:10.1016/0005-2736(83)90065-2

Biological membranes are rich in low-frequency motion

B. A. Cornell^*, R. G. Hiller, J. Raison, F. Separovic, R. Smith, J. C. Vary, C. Morris

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

33 Citations (Scopus)

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., T_1p becomes shorter).

Original language	English
Pages (from-to)	473-478
Number of pages	6
Journal	BBA - Biomembranes
Volume	732
Issue number	2
DOIs	https://doi.org/10.1016/0005-2736(83)90065-2
Publication status	Published - 27 Jul 1983

Keywords

Low-frequency motion
Membrane protein
NMR

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10.1016/0005-2736(83)90065-2

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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).",

keywords = "Low-frequency motion, Membrane protein, NMR",

author = "Cornell, {B. A.} and Hiller, {R. G.} and J. Raison and F. Separovic and R. Smith and Vary, {J. C.} and C. Morris",

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AU - Cornell, B. A.

AU - Hiller, R. G.

AU - Raison, J.

AU - Separovic, F.

AU - Smith, R.

AU - Vary, J. C.

AU - Morris, C.

PY - 1983/7/27

Y1 - 1983/7/27

N2 - 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).

AB - 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).

KW - Low-frequency motion

KW - Membrane protein

KW - NMR

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IS - 2

ER -

Biological membranes are rich in low-frequency motion

Abstract

Keywords

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