Preferential Interactions of Proteins with Solvent Components in Aqueous Amino Acid Solutions

Tipo de material: Texto

TextoSeries ; Archives of BioChemistry and Biophysics, 224(1), p.169-177, 1983Trabajos contenidos:

Arakawa, T
Timasheff, S.N

Recursos en línea:

Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx

Resumen: The preferential interactions of proteins with solvent components in concentrated amino acid solutions were measured by high-precision densimetry. Bovine serum al- bumin and lysozyme were preferentially hydrated in all of the amino acids examined, glycine, (Y- and /3-alanine, and betaine, i.e., addition of these amino acids resulted in an unfavorable free energy change. It was shown that, for the former three amino acids, known to have a positive surface tension increment, their perturbation of the surface free energy of water is consistent with their preferential exclusion from the protein surface. In the case of betaine, which does not increase the surface tension of water, preferential exclusion from protein surface must reflect the chemical structure of this cosolvent, which is considerably more hydrophobic than that of the other three amino acids.

Tags from this library: No tags from this library for this title. Log in to add tags.

Average rating: 0.0 (0 votes)

Holdings
Item type	Current library	Collection	Call number	Status	Date due	Barcode
Documentos solicitados	CICY Documento préstamo interbibliotecario	Ref1	B-14845 (Browse shelf(Opens below))	Available

Browsing CICY shelves, Shelving location: Documento préstamo interbibliotecario, Collection: Ref1 Close shelf browser (Hides shelf browser)

Previous	No cover image available	No cover image available	No cover image available	No cover image available	No cover image available	No cover image available	No cover image available	Next
Previous	B-14842 Agrigenomics for Microalgal Biofuel Production: An Overview of Various Bioinformatics Resources and Recent Studies to Link OMICS to Bioenergy and Bioeconomy	B-14843 The Influence of Hydroxyapatite Particles onIn Vitro Degradation Behavior of Polye-Caprolactone-Based Composite Scaffolds	B-14844 Constituents of Magnolia grandiflora; Cyclocolorenone	B-14845 Preferential Interactions of Proteins with Solvent Components in Aqueous Amino Acid Solutions	B-14846 Kodamaea ohmeri(Ascomycota: Saccharomycotina)presence in commercial Bombus impatiensCresson and feral Bombus pensylvanicusDeGeer (Hymenoptera: Apidae)colonies	B-14847 The irruption of polymers from renewable resources on the scene of macromolecular science and technology	B-14848 Electrocatalytic and Sensors Properties of Natural Smectite Type Clay towards the Detection of Paraquat Using a Film-Modified Electrode	Next

The preferential interactions of proteins with solvent components in concentrated amino acid solutions were measured by high-precision densimetry. Bovine serum al- bumin and lysozyme were preferentially hydrated in all of the amino acids examined, glycine, (Y- and /3-alanine, and betaine, i.e., addition of these amino acids resulted in an unfavorable free energy change. It was shown that, for the former three amino acids, known to have a positive surface tension increment, their perturbation of the surface free energy of water is consistent with their preferential exclusion from the protein surface. In the case of betaine, which does not increase the surface tension of water, preferential exclusion from protein surface must reflect the chemical structure of this cosolvent, which is considerably more hydrophobic than that of the other three amino acids.

There are no comments on this title.

to post a comment.