Citation: Irum Naureen, Aisha Saleem, Hafiza Hira Rehman, Umar farooq, Iqra Iqbal, Tayyaba Sehar, Tahir Ali (2022). Intrinsically Disordered Proteins, Structural and Functional Dynamics. Sch Int J Biochem, 5(1): 8-14. 8 Scholars International Journal of Biochemistry Abbreviated Key Title: Sch Int J Biochem ISSN 2616-8650 (Print) |ISSN 2617-3476 (Online) Scholars Middle East Publishers, Dubai, United Arab Emirates Journal homepage: https://saudijournals.com Review Article Intrinsically Disordered Proteins, Structural and Functional Dynamics Irum Naureen 1 , Aisha Saleem 2* , Hafiza Hira Rehman 2 , Umar farooq 2 , Iqra Iqbal 2 , Tayyaba Sehar 2 , Tahir Ali 2 1 Assistant Professor, School of Zoology, Minhaj University Lahore, Pakistan 2 M. Phil Researcher, School of Zoology, Minhaj University Lahore, Pakistan DOI: 10.36348/sijb.2022.v05i01.002 | Received: 11.12.2021 | Accepted: 16.01.2022 | Published: 21.01.2022 *Corresponding author: Aisha Saleem M. Phil Researcher, School of Zoology, Minhaj University Lahore, Pakistan Abstract The classical theory is that before being biologically active, proteins are assembled into a unique three-dimensional structure in terms of quality. These Intrinsically Disordered Proteins (IDPs) are very common in many genomes, including humans and play a key role in central cell processes such as transcription and translation, cell cycle, and cell signaling regulation. In addition, the proportion of proteins associated with various diseases such as cancer and neurodegenerative diseases is very high in IDPs. Therefore, considerable efforts have been made to elucidate the molecular mechanisms supporting the role of IDPs in Biology and disease through the use of experimental and computational methods. Animal models are needed for human genetic anatomy and better treatment options. Genetic disease Although some animals are used key models in academic and industrial research .There is a lot of stress in the anatomy of genetic diseases. The Genetic resemblance of rats and the humans from which is naturally occurring genetic disease, unique population. The availability of structure and complete genomic sequencing has made purebred dogs a powerful model. Used for disease research. The main advantage of dogs is that they suffer from about 450 genetic diseases, of which about half show significant medical symptoms, Similar to the same human disease. Therefore, these two facts make dogs an ideal medical practice, and a genetic model. This review sheds light on some of them, common genetic disease, in dog model. In this article plays an important role in identifying the genes responsible for the disease and / or the use of new genes, treatment of interest for dogs and humans. Keywords: Disordered proteins, Regulated unfolding, Muscular dystrophy. Copyright © 2022 The Author(s): This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International License (CC BY-NC 4.0) which permits unrestricted use, distribution, and reproduction in any medium for non-commercial use provided the original author and source are credited. INTRODUCTION After synthesis on the ribosome, most proteins are arranged in a unique three-dimensional structure, determined by the sequence of amino acids. This folding process is usually required for biological activity, whether it is artificial or with the help of molecular chaperone [1]. However, proteins studied at the molecular level are increasingly unrelated to the function of a single structure [2, 4]. In contrast, for this type of so-called Intrinsically Disordered Protein (IDP), the greatest feature of the natural state is the dynamic set of inter conversion conformation. In this case, the term "error" means lack of some stable three-dimensional structure. Many other terms, such as "unstructured" and "expanded" are also widely used to describe this phenomenon, but the name IDP is currently the most widely used for this type of protein. IDP structural disorders can occur in one or more separate areas along the strand, or they can spread over the entire length of the protein. The concept of defects in protein structure is not really new. For example, the peptide hormone [5] the "linker" that binds to the domains of a multi-domain protein, or the loop that binds to the secondary structural elements of other configured proteins, may have large amounts of structural heterogeneity [6]. There is X-ray crystallography experiments usually have gaps in the electron density map [7]. However, over the past decade, with the development of protein biophysical characterization techniques, particularly nuclear magnetic resonance (NMR) spectroscopy [8] and bioinformatics tools to predict disease directly from amino acid sequencing, it has two broad effects [9]. It is clear that protein deficiency is very common in many organisms, especially in complex organisms. In the bacterial genome, it is estimated that only 4% of all proteins contain chaotic regions that are at least 30 amino acids long, while the