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Hydration and interactions in protein solutions containing concentrated electrolytes studied by small-angle scattering

Zhang, F. ; Roosen-Runge, F. LU ; Skoda, M. W.A. ; Jacobs, R. M.J. ; Wolf, M. ; Callow, Ph ; Frielinghaus, H. ; Pipich, V. ; Prévost, S. and Schreiber, F. (2012) In Physical Chemistry Chemical Physics 14(7). p.2483-2493
Abstract

During protein crystallization and purification, proteins are commonly found in concentrated salt solutions. The exact interplay of the hydration shell, the salt ions, and protein-protein interactions under these conditions is far from being understood on a fundamental level, despite the obvious practical relevance. We have studied a model globular protein (bovine serum albumin, BSA) in concentrated salt solutions by small-angle neutron scattering (SANS). The data are also compared to previous studies using SAXS. The SANS results for dilute protein solutions give an averaged volume of BSA of 91700 3, which is about 37% smaller than that determined by SAXS. The difference in volume corresponds to the contribution of a... (More)

During protein crystallization and purification, proteins are commonly found in concentrated salt solutions. The exact interplay of the hydration shell, the salt ions, and protein-protein interactions under these conditions is far from being understood on a fundamental level, despite the obvious practical relevance. We have studied a model globular protein (bovine serum albumin, BSA) in concentrated salt solutions by small-angle neutron scattering (SANS). The data are also compared to previous studies using SAXS. The SANS results for dilute protein solutions give an averaged volume of BSA of 91700 3, which is about 37% smaller than that determined by SAXS. The difference in volume corresponds to the contribution of a hydration shell with a hydration level of 0.30 g g -1 protein. The forward intensity I(0) determined from Guinier analysis is used to determine the second virial coefficient, A 2, which describes the overall protein interactions in solution. It is found that A 2 follows the reverse order of the Hofmeister series, i.e. (NH 4) 2SO 4 < Na 2SO 4 < NaOAc < NaCl < NaNO 3 < NaSCN. The dimensionless second virial coefficient B 2, corrected for the particle volume and molecular weight, has been calculated using different approaches, and shows that B 2 with corrections for hydration and the non-spherical shape of the protein describes the interactions better than those determined from the bare protein. SANS data are further analyzed in the full q-range using liquid theoretical approaches, which gives results consistent with the A 2 analysis and the experimental structure factor.

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author
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publishing date
type
Contribution to journal
publication status
published
in
Physical Chemistry Chemical Physics
volume
14
issue
7
pages
11 pages
publisher
Royal Society of Chemistry
external identifiers
  • scopus:84863012197
  • pmid:22249363
ISSN
1463-9076
DOI
10.1039/c2cp23460b
language
English
LU publication?
no
id
c8d97516-5315-47b5-be5f-3c4f633b9159
date added to LUP
2018-12-17 09:49:01
date last changed
2025-06-25 11:13:27
@article{c8d97516-5315-47b5-be5f-3c4f633b9159,
  abstract     = {{<p>During protein crystallization and purification, proteins are commonly found in concentrated salt solutions. The exact interplay of the hydration shell, the salt ions, and protein-protein interactions under these conditions is far from being understood on a fundamental level, despite the obvious practical relevance. We have studied a model globular protein (bovine serum albumin, BSA) in concentrated salt solutions by small-angle neutron scattering (SANS). The data are also compared to previous studies using SAXS. The SANS results for dilute protein solutions give an averaged volume of BSA of 91700 <sup>3</sup>, which is about 37% smaller than that determined by SAXS. The difference in volume corresponds to the contribution of a hydration shell with a hydration level of 0.30 g g <sup>-1</sup> protein. The forward intensity I(0) determined from Guinier analysis is used to determine the second virial coefficient, A <sub>2</sub>, which describes the overall protein interactions in solution. It is found that A <sub>2</sub> follows the reverse order of the Hofmeister series, i.e. (NH <sub>4</sub>) <sub>2</sub>SO <sub>4</sub> &lt; Na <sub>2</sub>SO <sub>4</sub> &lt; NaOAc &lt; NaCl &lt; NaNO <sub>3</sub> &lt; NaSCN. The dimensionless second virial coefficient B <sub>2</sub>, corrected for the particle volume and molecular weight, has been calculated using different approaches, and shows that B <sub>2</sub> with corrections for hydration and the non-spherical shape of the protein describes the interactions better than those determined from the bare protein. SANS data are further analyzed in the full q-range using liquid theoretical approaches, which gives results consistent with the A <sub>2</sub> analysis and the experimental structure factor.</p>}},
  author       = {{Zhang, F. and Roosen-Runge, F. and Skoda, M. W.A. and Jacobs, R. M.J. and Wolf, M. and Callow, Ph and Frielinghaus, H. and Pipich, V. and Prévost, S. and Schreiber, F.}},
  issn         = {{1463-9076}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{7}},
  pages        = {{2483--2493}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Physical Chemistry Chemical Physics}},
  title        = {{Hydration and interactions in protein solutions containing concentrated electrolytes studied by small-angle scattering}},
  url          = {{http://dx.doi.org/10.1039/c2cp23460b}},
  doi          = {{10.1039/c2cp23460b}},
  volume       = {{14}},
  year         = {{2012}},
}