High pressure small-angle neutron scattering study of the aggregation state of ?-lactoglobulin in water and in water/ethylene-glycol solutions
High pressure small-angle neutron scattering study of the aggregation state of ?-lactoglobulin in water and in water/ethylene-glycol solutions
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? 2006 Elsevier Inc
Accession number: 8886404
Title: High pressure small-angle neutron scattering study of the aggregation state of ?-lactoglobulin in water and in water/ethylene-glycol solutions
Authors: Ortore, M.G.1 ; Spinozzi, F.1 ; Carsughi, F.1 ; Mariani, P.1 ; Bonetti, M.; Onori, G.
Author affiliation: 1 Dipt. di Sci. Applicate ai Sistemi Complessi, Univ. Politecnica delle Marche, Ancona, Italy
Serial title: Chemical Physics Letters
Abbreviated serial title: Chem. Phys. Lett. (Netherlands)
Volume: 418
Issue: 4-6
Publication date: 6 Feb. 2006
Pages: 342-6
Language: English
ISSN: 0009-2614
CODEN: CHPLBC
Document type: Journal article (JA)
Publisher: Elsevier
Country of publication: Netherlands
Material Identity Number: C027-2006-002
Abstract: High-pressure SANS experiments have been performed on acidic dilute solutions of the dimeric protein ?-lactoglobulin. To evidence the solvent effect on the protein stability during compression, two different solvents, D2O and a 50%w/w mixture of water and ethylene-glycol have been considered. Data confirm that pressure induces dissociation in both solvents, even if ?-lactoglobulin shows an higher stability in 50% ethylene-glycol. An original global fitting procedure has been used to derive the thermodynamic parameters that describe the dissociation equilibrium. As a result, the role of the solvent in protein dissociation has been observed to reflect on volume and compressibility changes. [All rights reserved Elsevier]
Number of references: 18
Inspec controlled terms: aggregation - biochemistry - biological techniques - compressibility - dissociation - heavy water - high-frequency effects - molecular biophysics - neutron diffraction - proteins - solvent effects
Uncontrolled terms: high pressure small-angle neutron scattering - aggregation state - dimeric protein ?-lactoglobulin - water-ethylene-glycol solutions - acidic dilute solutions - solvent effect - protein stability - D2O - global fitting procedure - thermodynamic parameters - protein dissociation equilibrium - compressibility
Inspec classification codes: A8715D Physical chemistry of biomolecular solutions; condensed states - A8715K Biomolecular interactions, charge transfer complexes - A8780 Biophysical instrumentation and techniques
Treatment: Experimental (EXP)
Discipline: Physics (A)
DOI: 10.1016/j.cplett.2005.11.019
Database: Inspec
Copyright 2006, The Institution of Engineering and Technology
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