Abstract

The functioning of native protein has been discussed briefly. Disruption in native protein with misfolding in its structure due to infection or otherwise has also been discussed .The physical characteristics of prion- a variety of protein responsible for number of both degenerative and non-degenerative diseases have been detailed here from the view point of protein vibration due to external stimuli. Attempts have been taken to focus on the effects of charge groups on the surface of both folded and misfolded protein. Suggestion for application of magnetic materials which may be able to create potential barrier in controlling the chain process of infectious prions and other similar proteins have also been discussed basing on the frequencies of vibration of protein and also on the vibration energy thus evaluated.

Highlights

  • Modern understanding of how proteins function emerges since last 200 years of biochemical studies

  • Translation helps in converting single dimension of the genetic code into three dimensional protein structures which is usually expressed in folded form

  • Under the above crucial junctures, the main thrust of this paper is to examine the physical characteristics of PrPc conversion into PrPsc which is responsible for a number of degenerative diseases and Transmissible Spongiform encephalopathies (TSEs) diseases from the view point of our hypothetical approach of protein vibration

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Summary

Introduction

Modern understanding of how proteins function emerges since last 200 years of biochemical studies. It may be held that proteins are proper components for cell function .Proteins as Hermann Staudinger held are organized polymers, giant molecules made of small molecular constituents linked each other by chemical bonds in chain. Proteins fold because of the fact that amino acids interact locally This limits the conformational space that a protein has to explore and to follow a funnel like energy landscape. Exposition of hydrophobic amino acid residues is found during abnormal conformational transition from alpha helix to beta sheet. It is an established fact that misfolded protein results when a protein follows the wrong way in its folding process Some of these are [3] listed below: Proteopathy

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