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PMID: 8650185 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Conformational trapping in a membrane environment: a regulatory mechanism for protein activity?

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 12 ·1996-06-11 ·Pages 5872-6

Arumugam S, Pascal S, North CL, Hu W, Lee KC, Cotten M, Ketchem RR, Xu F, Brenneman M, Kovacs F, Tian F, Wang A, Huo S, Cross TA

Abstract

Functional regulation of proteins is central to living organisms. Here it is shown that a nonfunctional conformational state of a polypeptide can be kinetically trapped in a lipid bilayer environment. This state is a metastable structure that is stable for weeks just above the phase transition temperature of the lipid. When the samples are incubated for several days at 68 degrees C, 50% of the trapped conformation converts to the minimum-energy functional state. This result suggests the possibility that another mechanism for functional regulation of protein activity may be available for membrane proteins: that cells may insert proteins into membranes in inactive states pending the biological demand for protein function.

MeSH Terms
Magnetic Resonance Spectroscopy Protein Conformation Proteins/chemistry,physiology
Chemicals
Proteins
Authors & Affiliations
14 authors, click to expand affiliations / ORCID
Arumugam S
Center for Interdisciplinary Magnetic Resonance at the National High Magnetic Field Laboratory, Institute of Molecular Biophysics, Florida State University, Tallahassee, 32306, USA.
Pascal S
North C L
Hu W
Lee K C
Cotten M
Ketchem R R
Xu F
Brenneman M
Kovacs F
Tian F
Wang A
Huo S
Cross T A
References (26)
26 references, click to expand
  1. The conformation of gramicidin A.
    Biochemistry. 1974 Dec 17;13(26):5249-56 PMID: 4139971
  2. Kinetics of gramicidin channel formation in lipid bilayers: transmembrane monomer association.
    Science. 1990 Nov 30;250(4985):1256-9 PMID: 1700867
  3. The effect of water on enzyme action in organic media.
    J Biol Chem. 1988 Jun 15;263(17):8017-21 PMID: 3131337
  4. Three-dimensional structure at 0.86 A of the uncomplexed form of the transmembrane ion channel peptide gramicidin A.
    Science. 1988 Jul 8;241(4862):188-91 PMID: 2455345
  5. NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
    Science. 1991 May 31;252(5010):1303-5 PMID: 1925542
  6. Enzymatic catalysis and dynamics in low-water environments.
    Proc Natl Acad Sci U S A. 1992 Feb 1;89(3):1100-4 PMID: 1310539
  7. Structure of an isolated gramicidin A double helical species by high-resolution nuclear magnetic resonance.
    J Mol Biol. 1992 Aug 20;226(4):1101-9 PMID: 1381444
  8. A conformational rearrangement in gramicidin A: from a double-stranded left-handed to a single-stranded right-handed helix.
    Biochemistry. 1992 Sep 22;31(37):8822-8 PMID: 1382580
  9. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR.
    Science. 1993 Sep 10;261(5127):1457-60 PMID: 7690158
  10. High-resolution structure and dynamic implications for a double-helical gramicidin A conformer.
    J Biomol NMR. 1993 Sep;3(5):495-513 PMID: 7693092
  11. Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy.
    Biophys J. 1994 Jan;66(1):14-24 PMID: 7510525
  12. Distorted structure of the retinal chromophore in bacteriorhodopsin resolved by 2H-NMR.
    Biochemistry. 1994 May 10;33(18):5370-5 PMID: 8180159
  13. Kinetics versus thermodynamics in protein folding.
    Biochemistry. 1994 Jun 21;33(24):7505-9 PMID: 8011615
  14. Structure and orientation of the pore-forming peptide, melittin, in lipid bilayers.
    J Mol Biol. 1994 Aug 19;241(3):456-66 PMID: 8064858
  15. A relationship between protein stability and protein function.
    Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):452-6 PMID: 7831309
  16. Transbilayer movement and net flux of cholesterol and cholesterol sulfate between liposomal membranes.
    Biochemistry. 1995 May 9;34(18):6208-17 PMID: 7742326
  17. Restatement of order parameters in biomembranes: calculation of C-C bond order parameters from C-D quadrupolar splittings.
    Biophys J. 1995 May;68(5):1727-39 PMID: 7612816
  18. The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes.
    Biochemistry. 1988 Jun 28;27(13):4848-55 PMID: 2458757
  19. Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
    Biophys J. 1988 Aug;54(2):259-67 PMID: 2462923
  20. HPLC study on the 'history' dependence of gramicidin A conformation in phospholipid model membranes.
    FEBS Lett. 1989 Jun 19;250(1):67-71 PMID: 2472295
  21. Solid phase peptide synthesis of 15N-gramicidins A, B, and C and high performance liquid chromatographic purification.
    Int J Pept Protein Res. 1989 Apr;33(4):298-303 PMID: 2473960
  22. Gramicidin cation channel: an experimental determination of the right-handed helix sense and verification of beta-type hydrogen bonding.
    Biochemistry. 1989 Nov 28;28(24):9379-85 PMID: 2482072
  23. Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing.
    Nature. 1990 May 3;345(6270):86-9 PMID: 2330057
  24. Membrane protein folding and oligomerization: the two-stage model.
    Biochemistry. 1990 May 1;29(17):4031-7 PMID: 1694455
  25. Gramicidin channels and pores.
    Annu Rev Biophys Biophys Chem. 1990;19:127-57 PMID: 1694667
  26. Conformation and molecular mechanisms of carriers and channels.
    Ann N Y Acad Sci. 1975 Dec 30;264:203-20 PMID: 56911
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.12.5872
Published
1996-06-11
Pages
5872-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC39154
Subset
IM
Grants
NIGMS NIH HHS · GM-4902 · United States
External Links
PubMed source DOI: 10.1073/pnas.93.12.5872 PMC Full Text View journal details
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