STUDY ON THE DESTABILIZATION OF LYSOZYME AND THE CHAPERONE-LIKE ACTIVITY OF ALPHA CRYSTALLIN

ABSTRACT

At different temperatures, the destabilization of Lysozyme and chaperone-like activity of alpha crystallin isolated from goat’s eye lenses were examined in phosphate buffer (pH 7.1) solution and dithiothretol (DTT). At 260 nm, this was spectrophotometrically observed. Alpha crystallin prevented the destabilization of lysozyme brought on by heat and DTT in a concentration-dependent manner. Like other chaperones, alpha crystallin performs its chaperone-like function by forming complexes to stop the aggregation of denatured proteins.

CHAPTER ONE

1.0 INTRODUCTION AND LITERATURE REVIEW

1.1 INTRODUCTION

The living cell’s workhorses are proteins. Despite the fact that proteins can vary in sequence, shape, and function, they all fold into the same stereo configuration, which is necessary for their proper function (Bruce et al., 2002). However, protein structures are not rigid; rather, they have a dynamic life style that includes complex association and dissociation, unfolding, and refolding (Anfisen, 1972). Proteins must either give up their structure or later regain it in response to stress and numerous physiological events. The native conformation of a protein, which makes up only a very small portion of the total configuration, is one of a very large number of distinct conformations for the polypeptide chain.

space. As a result, proteins’ amino acid sequences need to meet two criteria: one that is kinetic and the other that is thermodynamic. The sequence must have a distinctive folded conformation that is stable under physiological circumstances in order to meet the thermodynamic requirements.

Heat can denature the majority of proteins, which has complicated effects on the weak protein interactions (Vandenberg et al., 2000). A protein conformation typically remains intact when the temperature is gradually raised until an abrupt loss of structure and function happens over a limited temperature range (Nelson and Cox, 2008). A protein’s conformation is its atomic arrangement in space (Deechongkit et al., 2004).

 

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