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

INTRODUCTION

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

Chapter TWO

LITERATURE REVIEW

  • 2.1Introduction to Literature Review
  • 2.2Historical Perspectives
  • 2.3Theoretical Framework
  • 2.4Previous Studies on the Topic
  • 2.5Current Trends in Research
  • 2.6Gaps in Existing Literature
  • 2.7Conceptual Framework
  • 2.8Methodological Approaches
  • 2.9Emerging Technologies
  • 2.10Summary of Literature Review

Chapter THREE

RESEARCH METHODOLOGY

  • 3.1Introduction to Research Methodology
  • 3.2Research Design
  • 3.3Sampling Techniques
  • 3.4Data Collection Methods
  • 3.5Data Analysis Procedures
  • 3.6Ethical Considerations
  • 3.7Limitations of Methodology
  • 3.8Validation of Research Instruments

Chapter FOUR

DATA PRESENTATION AND ANALYSIS

  • 4.1Introduction to Discussion of Findings
  • 4.2Presentation of Data
  • 4.3Analysis of Results
  • 4.4Comparison with Hypotheses
  • 4.5Interpretation of Findings
  • 4.6Implications of Results
  • 4.7Recommendations for Future Research
  • 4.8Conclusion of Findings

Chapter FIVE

SUMMARY, CONCLUSION AND RECOMMENDATIONS

  • 5.1Conclusion and Summary

Project Abstract

<p> 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 <br></p>

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