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Study on the destabilization of lysozyme and the chaperone-like activity of alpha crystallin from sokoto red goat eye lens

 

Table Of Contents


Chapter ONE

1.1 Introduction
1.2 Background of Study
1.3 Problem Statement
1.4 Objective of Study
1.5 Limitation of Study
1.6 Scope of Study
1.7 Significance of Study
1.8 Structure of the Research
1.9 Definition of Terms

Chapter TWO

2.1 Overview of Lysozyme
2.2 Alpha Crystallin as a Chaperone
2.3 Destabilization of Lysozyme
2.4 Chaperone-Like Activity of Alpha Crystallin
2.5 Previous Studies on Lysozyme and Alpha Crystallin
2.6 Role of Chaperones in Protein Stability
2.7 Mechanisms of Protein Destabilization
2.8 Protein Folding and Misfolding
2.9 Interaction between Lysozyme and Alpha Crystallin
2.10 Comparative Analysis of Chaperone Activity

Chapter THREE

3.1 Research Methodology Overview
3.2 Selection of Lysozyme Samples
3.3 Purification of Alpha Crystallin
3.4 Experimental Setup for Destabilization Studies
3.5 Assays for Chaperone-Like Activity
3.6 Data Collection and Analysis Methods
3.7 Statistical Analysis Procedures
3.8 Ethical Considerations in Research

Chapter FOUR

4.1 Analysis of Destabilization Results
4.2 Evaluation of Chaperone Activity Assays
4.3 Comparison of Lysozyme Behavior
4.4 Insights into Alpha Crystallin Function
4.5 Correlation between Lysozyme Destabilization and Chaperone Activity
4.6 Discussion on Protein Stability Mechanisms
4.7 Implications of Findings in Biomedical Research
4.8 Future Research Directions

Chapter FIVE

5.1 Summary of Research Findings
5.2 Conclusion and Recommendations
5.3 Contribution to Scientific Knowledge
5.4 Practical Applications of the Study
5.5 Areas for Further Exploration

Thesis 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

Thesis Overview

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