Thermodynamics of target peptide recognition by calmodulin and a calmodulin analogue: implications for the role of the central linker

Moorthy, AK and Gopal, B and Satish, PR and Bhattacharya, S and Bhattacharya, A and Murthy, MRN and Surolia, A (1999) Thermodynamics of target peptide recognition by calmodulin and a calmodulin analogue: implications for the role of the central linker. In: FEBS-Letters, 461 (1-2). pp. 19-24.

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Abstract

The thermodynamics of interaction of two model peptides melittin and mastoparan with bovine brain calmodulin (CAM) and a smaller CAM analogue, a calcium binding protein from Entamoeba histolytica (CaBP) in 10 mM MOPS buffer (pH 7.0) was examined using isothermal titration calorimetry (ITC). These data show that CAM binds to both the peptides and the enthalpy of binding is endothermic for melittin and exothermic for mastoparan at 25oC. CaBP binds to the longer peptide melittin, but does not bind to mastoparan, the binding enthalpy being endothermic in nature. Concurrently, we also observe a larger increase in alpha-helicity upon the binding of melittin to CAM when compared to CaBP. The role of hydrophobic interactions in the binding process has also been examined using 8-anilino-1-naphthalene-sulphonic acid (ANS) binding monitored by ITC. These results have been employed to rationalize the energetic consequences of the binding reaction.

Item Type:	Journal Article
Publication:	FEBS-Letters
Publisher:	Elsevier Science B.V.
Additional Information:	This copyright belongs to Federation of European Biochemical Societies(FEBS Letters)
Keywords:	Calmodulin;Calcium binding protein;Isothermal titration calorimetry;Melittin;Mastoparan
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	27 Sep 2007
Last Modified:	19 Sep 2010 04:39
URI:	http://eprints.iisc.ac.in/id/eprint/11903

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