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Electron paramagnetic resonance spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apoA-I in solution

Lagerstedt, Jens O LU ; Budamagunta, Madhu S.; Oda, Michael N. and Voss, John C LU (2007) In Journal of Biological Chemistry 282(12). p.9-9143
Abstract

Apolipoprotein A-I (apoA-I) is the major protein constituent of high density lipoprotein (HDL) and plays a central role in phospholipid and cholesterol metabolism. This 243-residue long protein is remarkably flexible and assumes numerous lipid-dependent conformations. Consequently, definitive structural determination of lipid-free apoA-I in solution has been difficult. Using electron paramagnetic spectroscopy of site-directed spin labels in the N-terminal domain of apoA-I (residues 1-98) we have mapped a mixture of secondary structural elements, the composition of which is consistent with findings from other in-solution methods. Based on side chain mobility and their accessibility to polar and non-polar spin relaxers, the precise... (More)

Apolipoprotein A-I (apoA-I) is the major protein constituent of high density lipoprotein (HDL) and plays a central role in phospholipid and cholesterol metabolism. This 243-residue long protein is remarkably flexible and assumes numerous lipid-dependent conformations. Consequently, definitive structural determination of lipid-free apoA-I in solution has been difficult. Using electron paramagnetic spectroscopy of site-directed spin labels in the N-terminal domain of apoA-I (residues 1-98) we have mapped a mixture of secondary structural elements, the composition of which is consistent with findings from other in-solution methods. Based on side chain mobility and their accessibility to polar and non-polar spin relaxers, the precise location of secondary elements for amino acids 14-98 was determined for both lipid-free and lipid-bound apoA-I. Based on intermolecular dipolar coupling at positions 26, 44, and 64, these secondary structural elements were arranged into a tertiary fold to generate a structural model for lipid-free apoA-I in solution.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Apolipoprotein A-I, Crystallization, Dimerization, Electron Spin Resonance Spectroscopy, Humans, Lipids, Models, Molecular, Molecular Conformation, Mutagenesis, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Spin Labels, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
in
Journal of Biological Chemistry
volume
282
issue
12
pages
9 - 9143
publisher
ASBMB
external identifiers
  • scopus:34247857427
ISSN
0021-9258
DOI
10.1074/jbc.M608717200
language
English
LU publication?
no
id
f3c821e1-f0ea-4245-984f-e7d72221cfcf
date added to LUP
2017-10-19 20:10:41
date last changed
2017-10-23 09:56:27
@article{f3c821e1-f0ea-4245-984f-e7d72221cfcf,
  abstract     = {<p>Apolipoprotein A-I (apoA-I) is the major protein constituent of high density lipoprotein (HDL) and plays a central role in phospholipid and cholesterol metabolism. This 243-residue long protein is remarkably flexible and assumes numerous lipid-dependent conformations. Consequently, definitive structural determination of lipid-free apoA-I in solution has been difficult. Using electron paramagnetic spectroscopy of site-directed spin labels in the N-terminal domain of apoA-I (residues 1-98) we have mapped a mixture of secondary structural elements, the composition of which is consistent with findings from other in-solution methods. Based on side chain mobility and their accessibility to polar and non-polar spin relaxers, the precise location of secondary elements for amino acids 14-98 was determined for both lipid-free and lipid-bound apoA-I. Based on intermolecular dipolar coupling at positions 26, 44, and 64, these secondary structural elements were arranged into a tertiary fold to generate a structural model for lipid-free apoA-I in solution.</p>},
  author       = {Lagerstedt, Jens O and Budamagunta, Madhu S. and Oda, Michael N. and Voss, John C},
  issn         = {0021-9258},
  keyword      = {Apolipoprotein A-I,Crystallization,Dimerization,Electron Spin Resonance Spectroscopy,Humans,Lipids,Models, Molecular,Molecular Conformation,Mutagenesis,Protein Binding,Protein Conformation,Protein Folding,Protein Structure, Secondary,Protein Structure, Tertiary,Spin Labels,Journal Article,Research Support, N.I.H., Extramural,Research Support, Non-U.S. Gov't},
  language     = {eng},
  month        = {03},
  number       = {12},
  pages        = {9--9143},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Electron paramagnetic resonance spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apoA-I in solution},
  url          = {http://dx.doi.org/10.1074/jbc.M608717200},
  volume       = {282},
  year         = {2007},
}