Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/48183
Title: Protein loop compaction and the origin of the effect of arginine and glutamic acid mixtures on solubility, stability and transient oligomerization of proteins
Author: Blobel, Jascha
Brath, Ulrika
Bernadó i Peretó, Pau
Diehl, Carl
Ballester, Lidia
Sornosa, Alejandra
Akke, Mikael
Pons Vallès, Miquel
Keywords: Proteïnes
Macromolècules
Estabilitat
Electròlits
Solubilitat
Oligòmers
Polielectròlits
Proteins
Macromolecules
Stability
Electrolytes
Solubility
Oligomers
Polyelectrolytes
Issue Date: 2011
Publisher: Springer Verlag
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.
Note: Versió postprint del document publicat a: http://dx.doi.org/10.1007/s00249-011-0686-3
It is part of: European Biophysics Journal With Biophysics Letters, 2011, vol. 40, num. 12, p. 1327-1338
Related resource: http://dx.doi.org/10.1007/s00249-011-0686-3
URI: http://hdl.handle.net/2445/48183
ISSN: 0175-7571
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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