Journal of Diabetes & Clinical Practice
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  • Mini Review   
  • J Diabetes Clin Prac 2023, Vol 6(3): 190
  • DOI: 10.4172/jdce.1000190

Proteins that have been Myristoylated and are Intrinsically Disordered Change in Structure and Hydration

Kikung Hehelo*
Department of Diabetology and Molecular Biology, University of Botswana, Botswana
*Corresponding Author : Kikung Hehelo, Department of Diabetology and Molecular Biology, University of Botswana, Botswana, Email: hehelokikung@gmail.com

Received Date: Apr 10, 2023 / Accepted Date: May 03, 2023 / Published Date: May 08, 2023

Abstract

Post-translational modifications play a crucial role in modulating the structure and function of proteins. Myristoylation, the attachment of a myristoyl group to the N-terminus of a protein, is a common modification that facilitates membrane association. While the effects of myristoylation on structured proteins have been extensively studied, its impact on intrinsically disordered proteins (IDPs) remains less explored. This abstract highlights the changes in structure and hydration of myristoylated IDPs. Intrinsically disordered proteins are a class of proteins that lack a well-defined structure but possess critical biological functions. Myristoylation can induce structural changes in IDPs by promoting the formation of transient secondary structure elements or modulating local folding propensity. The myristoyl group's presence can alter the conformational dynamics of IDPs, resulting in the adoption of specific structural motifs upon membrane binding. Additionally, myristoylation can facilitate protein-protein interactions, leading to changes in the overall structure of IDPs. Hydration, an essential factor for protein stability and function, is also affected by myristoylation in IDPs. Experimental studies have shown that myristoylated IDPs exhibit distinct hydration dynamics compared to their non-myristoylated counterparts. The myristoyl group can influence the hydration of specific regions of the IDP by shielding them from solvent exposure, while other regions may experience enhanced hydration. These hydration changes have implications for the interactions of myristoylated IDPs with partner proteins and membranes.

Citation: Hehelo K (2023) Proteins that have been Myristoylated and are Intrinsically Disordered Change in Structure and Hydration. J Diabetes Clin Prac 6: 190. Doi: 10.4172/jdce.1000190

Copyright: © 2023 Hehelo K. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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