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Amino acid transport in thermophiles: Characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability

Paper ID Volume ID Publish Year Pages File Format Full-Text
30721 44498 2013 8 PDF Available
Title
Amino acid transport in thermophiles: Characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability
Abstract

Arginine-binding protein from Thermotoga maritima (TmArgBP) is a 27.7 kDa protein possessing the typical two domain structure of the periplasmic binding protein family. The protein is characterized by high specificity and affinity for binding a single molecule of l-arginine.In this work, the effect of temperature and/or guanidine hydrochloride on structure and stability of the protein in the absence and in the presence of l-arginine has been investigated by differential scanning calorimetry, far-UV circular dichroism and intrinsic tryptophan phosphorescence and fluorescence. The results revealed that TmArgBP undergoes an irreversible one-step thermal unfolding process in a cooperative mode. The TmArgBP melting temperature was recorded at 115 °C. The presence of l-arginine did not change the protein secondary structure content as well as the intrinsic phosphorescence and fluorescence protein properties, even if it increases the structural stability of the protein.The obtained results are discussed in combination with a detailed inspection of the three-dimensional structure of the protein.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► TmArgBP secondary structure content does not reveal differences when the protein binds to l-arginine. ► Thermal unfolding of TmArgBP occurs through a cooperative one-step process. The Tm of TmArgBP has been recorded at 115 °C. ► The presence of l-arginine stabilizes TmArgBP structure increasing the Tm of 4 °C. ► The protein does not report changes in fluorescence and phosphorescence emission upon ligand binding. ► Thermodynamic parameters of the denaturation of TmArgBP at pH 7.0, in the absence and in the presence of l-arginine.

Keywords
Fluorescence; Phosphorescence; Arginine; Extremophiles; Unfolding; Thermodynamics
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Amino acid transport in thermophiles: Characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 118, 5 January 2013, Pages 66–73
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