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Protein loop compaction and the origin of the effect of arginine and glutamic acid mixtures on solubility, stability and transient oligomerization of proteins

Blobel, Jascha; Brath, Ulrika LU ; Bernado, Pau; Diehl, Carl LU ; Ballester, Lidia; Sornosa, Alejandra; Akke, Mikael LU and Pons, Miquel (2011) In European Biophysics Journal 40(12). p.1327-1338
Abstract
Addition of a 50 mM mixture of l-arginine and l-glutamic acid (RE) is extensively used to improve protein solubility and stability, although the origin of the effect is not well understood. We present Small Angle X-ray Scattering (SAXS) and Nuclear Magnetic Resonance (NMR) results showing that RE induces protein compaction by collapsing flexible loops on the protein core. This is suggested to be a general mechanism preventing aggregation and improving resistance to proteases and to originate from the polyelectrolyte nature of RE. Molecular polyelectrolyte mixtures are expected to display long range correlation effects according to dressed interaction site theory. We hypothesize that perturbation of the RE solution by dissolved proteins is... (More)
Addition of a 50 mM mixture of l-arginine and l-glutamic acid (RE) is extensively used to improve protein solubility and stability, although the origin of the effect is not well understood. We present Small Angle X-ray Scattering (SAXS) and Nuclear Magnetic Resonance (NMR) results showing that RE induces protein compaction by collapsing flexible loops on the protein core. This is suggested to be a general mechanism preventing aggregation and improving resistance to proteases and to originate from the polyelectrolyte nature of RE. Molecular polyelectrolyte mixtures are expected to display long range correlation effects according to dressed interaction site theory. We hypothesize that perturbation of the RE solution by dissolved proteins is proportional to the volume occupied by the protein. As a consequence, loop collapse, minimizing the effective protein volume, is favored in the presence of RE. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Protein compaction, Crowding, Molecular polyelectrolytes, Loop, dynamics, Protein stability, Co-solutes
in
European Biophysics Journal
volume
40
issue
12
pages
1327 - 1338
publisher
Springer
external identifiers
  • wos:000297367100006
  • scopus:82455171921
ISSN
0175-7571
DOI
10.1007/s00249-011-0686-3
language
English
LU publication?
yes
id
7015f52d-f8a7-4fc5-93d2-d6372b13bcd2 (old id 2272133)
date added to LUP
2011-12-29 13:11:33
date last changed
2017-08-20 03:54:13
@article{7015f52d-f8a7-4fc5-93d2-d6372b13bcd2,
  abstract     = {Addition of a 50 mM mixture of l-arginine and l-glutamic acid (RE) is extensively used to improve protein solubility and stability, although the origin of the effect is not well understood. We present Small Angle X-ray Scattering (SAXS) and Nuclear Magnetic Resonance (NMR) results showing that RE induces protein compaction by collapsing flexible loops on the protein core. This is suggested to be a general mechanism preventing aggregation and improving resistance to proteases and to originate from the polyelectrolyte nature of RE. Molecular polyelectrolyte mixtures are expected to display long range correlation effects according to dressed interaction site theory. We hypothesize that perturbation of the RE solution by dissolved proteins is proportional to the volume occupied by the protein. As a consequence, loop collapse, minimizing the effective protein volume, is favored in the presence of RE.},
  author       = {Blobel, Jascha and Brath, Ulrika and Bernado, Pau and Diehl, Carl and Ballester, Lidia and Sornosa, Alejandra and Akke, Mikael and Pons, Miquel},
  issn         = {0175-7571},
  keyword      = {Protein compaction,Crowding,Molecular polyelectrolytes,Loop,dynamics,Protein stability,Co-solutes},
  language     = {eng},
  number       = {12},
  pages        = {1327--1338},
  publisher    = {Springer},
  series       = {European Biophysics Journal},
  title        = {Protein loop compaction and the origin of the effect of arginine and glutamic acid mixtures on solubility, stability and transient oligomerization of proteins},
  url          = {http://dx.doi.org/10.1007/s00249-011-0686-3},
  volume       = {40},
  year         = {2011},
}