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Glycine Betaine Interactions with Proteins: Insights from Volume and Compressibility Measurements.
MedLine Citation:
PMID:  23293944     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
We report the first application of volume and compressibility measurements to characterization of interactions between cosolvents (osmolytes) and globular proteins. Specifically, we measure the partial molar volumes and adiabatic compressibilities of cytochrome c, ribonuclease A, lysozyme, and ovalbumin in aqueous solutions of the stabilizing osmolyte glycine betaine (GB) at concentrations between 0 and 4 M. The fact that globular proteins do not undergo any conformational transitions in the presence of GB provides an opportunity to study the interactions of GB with proteins in their native states within the entire range of experimentally accessible GB concentrations. We analyze our resulting volumetric data within the framework of a statistical thermodynamic model in which each instance of GB interaction with a protein is viewed as a binding reaction that is accompanied by release of four water molecules. From this analysis, we calculate the association constants, k, as well as changes in volume, V0, and adiabatic compressibility, KS0, accompanying each GB-protein association event in an ideal solution. By comparing these parameters with the similar characteristics (k, V0, and KS0) determined for low molecular weight analogs of proteins, we conclude that there are no significant cooperative effects involved in GB interactions with any of the proteins studied in this work. We also evaluate the free energies of direct GB-protein interactions. The energetic properties of GB-protein association appear to scale with the size of the protein. For all proteins, the highly favorable change in free energy associated with direct protein-cosolvent interactions is nearly compensated by an unfavorable free energy of cavity formation (excluded volume effect) to yield a modestly unfavorable free energy of the transfer of a protein from water to a GB-water mixture.
Authors:
Yuen Lai Shek; Tigran V Chalikian
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-8
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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