Showing posts with label intrinsically disordered proteins. Show all posts
Showing posts with label intrinsically disordered proteins. Show all posts

Tuesday, 9 September 2025

Intrinsic Disorder Contribution to Open Reading Frame 4: Implications in Regulation & Pathogenesis of HEV | Chapter 3 | Shedding Light on the Open Reading Frame 4 of Hepatitis E Virus - Molecular, Evolutionary & Genetic Aspects

 

Due to insufficiency in appropriate hepatitis E virus (HEV) in vitro cell culture systems, our knowledge of its pathogenesis is inadequately understood. Viral proteins entail disordered regions that are linked with the infectivity and pathogenicity of the virus. Despite the general belief that unique biological functions of proteins require unique 3D structures (which dominated protein science for more than a century), structure-less intrinsically disordered proteins (IDPs)/intrinsically disordered protein regions (IDPRs) are functional, being able to engage in biological activities and perform impossible tricks that are highly unlikely for ordered proteins. The distribution of intrinsically disordered regions (IDRs) in the ORF4 protein is of great importance in the regulation of HEV. Thus, we examined the unstructured regions (IDRs) of this additional reading frame encoded protein ORF4, completely embedded inside ORF1, by analysing its IDRs, by exploiting computational methodologies. Our findings suggested that ORF4 had the prevalence of disordered regions. IDPRs are characterized by remarkable conformational flexibility and structural plasticity resulting in their engagement in several biological processes. In this chapter, some wonders of intrinsic disorder contribution to ORF4’s functions have been discussed.

 

Author(s) Details

 

Zoya Shafat

Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India.

 

Please see the link:- https://doi.org/10.9734/bpi/mono/978-81-976007-3-9/CH3

Tuesday, 25 May 2021

The Greatest Error in Biological Sciences, Started in 1930 and Continuing Up to Now, Generating Numerous Profound Misunderstandings in Almost All Fields of Biology | Chapter 13 | Current Advances in Chemistry and Biochemistry Vol. 5

 Is a cell a complex coacervate with distribution coefficients and adsorption coefficients as the primary physical–chemical characteristics, allowing for low-entropy bioenergetics based on coherence, as Schrödinger proposed in 1944? Is it possible that a cell contains ordinary water in solution with tiny solutes like K+, separated by a membrane containing ion-pumps that must constantly combat passive leaks? The latter viewpoint is known as "membrane-(pump)-theory" (MPT), which is still widely accepted in modern physiology and cell biology but contradicts numerous recent findings on intrinsically disordered proteins, membrane-less organelles, living systems' (quantum) coherence, and a slew of other key findings. It is not often known that during the 1960s and 1970s, Ling totally falsified MPT and produced an adsorption and coherence-based coacervate model for the live cell, complete with a set of experimentally confirmed new equations. All of the fundamental aspects of his so-called "association-induction-hypothesis" (AIH) have been proven in the lab. The goal of this paper is to show that the AIH is a good guide for interpreting many current physiological, physical-chemical, and physical data of live cells and sub-cellular systems, particularly those on coherent behaviour, that are incompatible with MPT. It will be demonstrated why we urgently require Ling's new bio-energetics and must reject MPT.

Author(s) Details

Laurent Jaeken
Department of Applied Engineering, Karel de Grote University College, Antwerp University Association, Antwerp, Belgium.

View Book :- https://stm.bookpi.org/CACB-V5/article/view/1095