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Insight Into the Early Stages of Thermal Unfolding of Peanut Agglutinin by Molecular Dynamics Simulations by Priti Hansia; Sagarika Dev; Avadhesha Surolia; Saraswathi Vishveshwara is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Peanut agglutinin is a homotetrameric nonglycosylated protein. The protein has a unique open quaternary structure. Molecular dynamics simulations have been employed to follow the atomistic details of its unfolding at different temperatures. The early events of the deoligomerization of the protein have been elucidated in the present study. Simulation trajectories of the monomer as well as those of the tetramer have been compared and the tetramer is found to be substantially more stable than its monomeric counterpart. The tetramer shows retention of most of its secondary structure but considerable loss of the tertiary structure at high temperature. This observation implies the generation of a molten globule‐like intermediate in the later stages of deoligomerization. The quaternary structure of the protein has weakened to a large extent, but none of the subunits are separated. In addition, the importance of the metal‐binding to the stability of the protein structure has also been investigated. Binding of the metal ions not only enhances the local stability of the metal‐ion binding loop, but also imparts a global stability to the overall structure. The dynamics of different

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Author

Priti Hansia; Sagarika Dev; Avadhesha Surolia; Saraswathi Vishveshwara

Publisher

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

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)