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The Structure, Molecular Dynamics, and Energetics of Centrin–melittin Complex by Liliana del Valle Sosa; Elisa Alfaro; Jorge Santiago; Daniel Narváez; Marie Cely Rosado; Aslin Rodríguez; Ana María Gómez; Eric R. Schreiter; Belinda Pastrana‐Ríos is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Centrin is a calcium binding protein (CaBP) belonging to the EF‐hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study __Chlamydomonas reinhardtii__ centrin (__Cr__cen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin–MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define __Cr__cen–MLT complex formation. Two‐dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I′, I′\*, and side chain bands for ^13^C‐__Cr__cen, MLT, and the ^13^C‐__Cr__cen–MLT complex. This approach resulted in the determination of MLT's increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin–MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP–MLT complex by X‐ray

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Author

Liliana del Valle Sosa; Elisa Alfaro; Jorge Santiago; Daniel Narváez; Marie Cely Rosado; Aslin Rodríguez; Ana María Gómez; Eric R. Schreiter; Belinda Pastrana‐Ríos

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2011

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)