Protein loop compaction and the origin of the effect of arginine and glutamic acid mixtures on solubility, stability and transient oligomerization of proteins
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2272133
- author
- Blobel, Jascha ; Brath, Ulrika LU ; Bernado, Pau ; Diehl, Carl LU ; Ballester, Lidia ; Sornosa, Alejandra ; Akke, Mikael LU and Pons, Miquel
- organization
- publishing date
- 2011
- 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
- pmid:21390527
- 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
- 2016-04-01 13:15:03
- date last changed
- 2022-02-19 03:46:07
@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}}, keywords = {{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}}, doi = {{10.1007/s00249-011-0686-3}}, volume = {{40}}, year = {{2011}}, }