Home » Bio-Chemistry » STUDY ON THE DESTABILIZATION OF LYSOZYME AND THE CHAPERONE-LIKE ACTIVITY OF ALPH...

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

Sold By: Joe Project Store | Item Type: Project Material | Report this?  |  Attributes: 50 pages | 1-5 chapters | Amount: ₦5,000 | Marked useful: 7,273 times

Delivery: Within 24 hours


ABSTRACT

Destabilization of Lysozyme and chaperone like action of alpha crystallin isolated from goat’s eye lens was investigated at various temperature ranges in phosphate buffer (pH 7.1) solution and dithiothretol (DTT). This was monitored spectrophotometrically at 260nm. The heat and DTT-induced destabilization of lysozyme was prevented by alpha crystallin in a concentration dependent manner. Alpha crystallin like other chaperones, fulfils its chaperone like action in preventing aggregation of denatured proteins by the formation of complexes.

CHAPTER ONE

1.0 INTRODUCTION AND LITERATURE REVIEW

1.1 INTRODUCTION

Proteins are the workhorses of the living cell. Although proteins may differ in sequence, shape and function, but have in common, the same stereo configuration (i.e. they all have to fold into specific three-dimensional structures) which are mandatory for proper function (Bruce et al., 2002). Protein structures however are not rigid, but have a dynamic life style, which may involve unfolding and refolding, complex association and dissociation (Anfisen, 1972). Stress and also many physiological events require proteins to surrender their structure or to regain it at a later stage. A very large number of distinct conformations exist for the polypeptide chain of which a protein spends most of its time in the native conformation, which spans only an extremely small fraction of the entire configuration space. Thus, the amino acid sequence of proteins must satisfy two requirements: one, thermodynamics and the other kinetic. The thermodynamics requirement is that the sequence must have a unique folded conformation, which is stable under physiological conditions.

Most proteins can be denatured by heat, which has complex effect on the weak interactions in proteins (Vandenberg et al., 2000). If the existing temperature is increased slowly, a protein conformation generally remains intact until an abrupt loss of structure and function occurs over a narrow temperature range (Nelson and Cox, 2008). The spatial arrangement of atoms in a protein is called its conformation (Deechongkit et al., 2004). 


Tags: Impact of study Destabilizatiuon of enzyme Destabilization of lysozyme Destabilization of alpha crystallin Importance of an enzyme

This material content is developed to serve as a GUIDE for students to conduct academic research
Find What You Want By Category:
Assignments
Business Plans
e-Books
Journals
Project Materials
Proposals
Seminar Reports
Term Papers

Delivery: Within 24 hours

Advertise Here

For advertisement, call 08168958821

Not what you were looking for? Perform a search

What's your project topic?

Comment on Facebook:

See More Bio-Chemistry Final Year Research Project Topics & Materials In PDF & Doc | iproject

More Project Material Departments