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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).
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SIMILAR BIOCHEMISTRY FINAL YEAR PROJECT RESEARCH TOPICS
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1. CARDIO PROTECTIVE ACTIVITIES OF N-HEXANE EXTRACT OF DESMODIUM VELUTINUM STEM ON ALBINO WISTER RAT
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» ABSTRACT The effect of ethanolic leaf extract of Sphenocentrum jollyanum pierre (SPJ) on liver function and hematological indices of cadmium chloride ...Continue Reading »Item Type & Format: Project Material - Ms Word | 52 pages | Instant Download | Chapter 1-5 | BIOCHEMISTRY DEPARTMENT
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3. EFFECTS OF ETHANOL ROOTS EXTRACT OF UGU OYIBO (Jatropha tanjorensis) ON HAEMATOLOGICAL INDICES OF FEMALE ALBINO WISTAR RATS
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4. EVALUATION OF THYROID DYSFUNCTION IN TYPE 2DIABETIC PATIENTS IN SOKOTO METROPOLIS
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5. ANTI-SCHIZOPHRENIC EFFECT OF METHANOL LEAVE EXTRACT OF INDIGOFERA ARRECTA IN ALBINO MICE
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6. EXTRACTION AND CHARACTERIZATION OF VEGETABLE OIL USING BREAD FRUIT SEED.
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7. EFFECTS OF BITTER LEAF SOUP WITH GARRI ON BLOOD GLUCOSE AND GROWTH PERFORMANCES OF TYPE ONESTZ [STREPTOZOCIN] INDUCED DIABETIC RATS
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8. PROXIMATE AND PHYSICOCHEMICAL ANALYSIS OF FISH FLOUR OBTAINED FROM THREE FISH SPECIES
» ABSTRACT Work on production proximate and physicochemical analyses of fish flour produced from Tilapia, cat and stock fishes was investigated. The fis...Continue Reading »Item Type & Format: Project Material - Ms Word | 52 pages | Instant Download | Chapter 1-5 | BIOCHEMISTRY DEPARTMENT
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9. DETERMINATION OF ACTIVE SWEET COMPONENTS OF COMMON ARTIFICIAL SWEETENERS THAT ARE USED AS REPLACEMENT FOR SUGAR
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10. EFFECT OF FRYING AND BOILING ON PHYSICOCHEMICAL PROPERTIES OF OIL
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