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Evaluation of carboxylic acid-induced conformational transitions of β-lactoglobulin: Comparison of the alcohol effects on β-lactoglobulin

Paper ID Volume ID Publish Year Pages File Format Full-Text
4981 265 2006 8 PDF Available
Title
Evaluation of carboxylic acid-induced conformational transitions of β-lactoglobulin: Comparison of the alcohol effects on β-lactoglobulin
Abstract

Conformational transitions of bovine β-lactoglobulin A (β-LG) induced by carboxylic acid were systematically studied by steady-state tryptophan (Trp) fluorescence. The behavior of β-LG denaturation depends upon the species and concentration of carboxylic acid, as well as on the pH of solutions. The order of the effectiveness of the respective carboxylic acids was described as follows: MeCOOH < EtCOOH < PrCOOH < ClEtCOOH < TFA < iBuCOOH < nBuCOOH < PFPA. The conformational change of β-LG through the carboxylic acid-induced transitions of the β-LG conformation were analyzed assuming a two-state mechanism between unfold and native states in order to obtain the m value, a measure of the dependence of the free energy change on the concentration of carboxylic acid. The m values of various carboxylic acids were compared with those of various alcohols based on the role of each group constituting the carboxylic acid and alcohol molecules, namely, the hydrocarbon group, hydroxyl group, halogen substituents, and the carboxyl group. Among these groups, the hydrophobic hydrocarbon groups and halogen substituents contributed positively to the m value, whereas the hydrophilic carboxyl and hydroxyl group contributed negatively. The present results can therefore be interpreted as a simple correlation based on the accessible surface area (ASA) of each groups of carboxylic acids and alcohols. These results suggest that the conformational transition of the protein due to the addition of carboxylic acids and alcohols can be explained both by hydrophobicity as well as clustering effects of each carboxylic acid and alcohol molecule.

Keywords
ASA, accessible surface area; PFPA, pentafluoropropionic acid; Trp, tryptophan; Cm, midpoint concentration; β-LG, β-lactoglobulin; ΔG, Gibbs free energyβ-Lactoglobulin; Unfolding; Carboxylic acid; Alcohol; Accessible surface area; Cluster formation
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Evaluation of carboxylic acid-induced conformational transitions of β-lactoglobulin: Comparison of the alcohol effects on β-lactoglobulin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 28, Issue 1, February 2006, Pages 79–86
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us