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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/11677

Title: Amino acids and short peptides do not always stabilize globular proteins: A differential scanning calorimetric study on their interactions with bovine alpha-lactalbumin
Authors: SABULAL, B
KISHORE, N
Keywords: preferential interactions
disulfide bonds
lysozyme
osmolyte
binding
water
Issue Date: 1997
Publisher: ROYAL SOC CHEMISTRY
Citation: JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS, 93(3), 433-436
Abstract: Amino acids and related compounds have been shown to confer stabilization to proteins; however, the generalization of such a statement is far from reality as there is a lack of experimental data on the interactions of amino acids and short peptides with different proteins. In particular, there are only a few reports(1-3) on direct differential calorimetric studies on these systems. Using DSC, we have studied the thermal denaturation of bovine alpha-lactalbumin in the presence-of-glycine, alanine, leucine, lysine, aspartic acid, glutamic acid, diglycine, triglycine, tetraglycine, pentaglycine, glycyl-leucine and glycyl-glycyl-leucine at neutral pH. It has been observed that these amino acids and peptides either do not provide thermal stabilization to a-lactalbumin or that the extent of stabilization is negligibly small. However, sucrose was able to confer thermal stability at neutral pH. All the thermal denaturations were-found to be two-state (i.e. natured reversible arrow denatured) and reversible and provide quantitative thermodynamic parameters associated with them. The results have been interpreted in terms of a fine balance between the preferential exclusion and binding which takes place during the course of the denaturation reaction. It follows from this study that the amino acids and peptides do not always stabilize globular proteins.
URI: http://dx.doi.org/10.1039/a605798e
http://dspace.library.iitb.ac.in/xmlui/handle/10054/11677
http://hdl.handle.net/10054/11677
ISSN: 0956-5000
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