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Probing protein surface accessibility of amino acid substitutions using hydrophobic interaction chromatography.

Becker, Kristian LU ; Grey, Marie LU and Bülow, Leif LU (2008) In Journal of Chromatography A 1215(1-2). p.152-155
Abstract
Hydrophobic interaction chromatography (HIC) has been used to determine the influence of amino acid substitutions on protein retention and thereby their accessibility on the protein surface. The retentions of mutants of green fluorescent protein (GFPuv) and human hemoglobin (Hb) were studied on multimodal HIC media and compared to the hydrophobicities from known hydrophobicity scales with respect to the accessible surface area. For GFPuv, the theoretical and experimental results of three hydrophobicity scales correlated well (R(2)>0.85), which clearly indicate that the results can be used for protein retention prediction as well as probing surface properties of protein variants.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Chromatography A
volume
1215
issue
1-2
pages
152 - 155
publisher
Elsevier
external identifiers
  • wos:000261845500019
  • pmid:19022452
  • scopus:56949108246
ISSN
0021-9673
DOI
10.1016/j.chroma.2008.11.002
language
English
LU publication?
yes
id
4de870f8-5791-4df9-963b-70962d6cffec (old id 1271261)
date added to LUP
2009-01-22 16:27:58
date last changed
2017-01-01 05:22:14
@article{4de870f8-5791-4df9-963b-70962d6cffec,
  abstract     = {Hydrophobic interaction chromatography (HIC) has been used to determine the influence of amino acid substitutions on protein retention and thereby their accessibility on the protein surface. The retentions of mutants of green fluorescent protein (GFPuv) and human hemoglobin (Hb) were studied on multimodal HIC media and compared to the hydrophobicities from known hydrophobicity scales with respect to the accessible surface area. For GFPuv, the theoretical and experimental results of three hydrophobicity scales correlated well (R(2)>0.85), which clearly indicate that the results can be used for protein retention prediction as well as probing surface properties of protein variants.},
  author       = {Becker, Kristian and Grey, Marie and Bülow, Leif},
  issn         = {0021-9673},
  language     = {eng},
  number       = {1-2},
  pages        = {152--155},
  publisher    = {Elsevier},
  series       = {Journal of Chromatography A},
  title        = {Probing protein surface accessibility of amino acid substitutions using hydrophobic interaction chromatography.},
  url          = {http://dx.doi.org/10.1016/j.chroma.2008.11.002},
  volume       = {1215},
  year         = {2008},
}