Course Content
Microscopes and Microscopy
MICROSCOPES AND MICROSCOPY OBJECTIVES By the end of this topic, the trainee should be able to: 1.Name various types of microscopes. 2.State the function of parts of a microscope. 3.Describe the use of compound light microscopes describe care and maintenance of compound microscopes. 4.Describe preparation of microscope slides
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The Cell
OBJECTIVES By the end of this topic, the trainee should be able to: 1.Define and explain meaning of terms. 2.State types of cells. 3.Describe the cell structure under the light microscope. 4.State the functions of cell organelles. 5.Describe the process of mitosis and meiosis. 6.Describe physiological processes of cells. 7.describe the techniques of cell isolation. 8.Describe the procedure of temporary cell preparation.
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Microorganisms
OBJECTIVES By the end of this topic , the trainee should be able to: 1.Classify the major groups of microorganisms. 2.State the general characteristics of each group. 3.Explain their mode of nutrition and reproduction. 4.Describe culture media. 5.Describe culturing techniques for bacteria. 6.Describe methods for determining bacteria population. 7.Describe sterilization and disinfection techniques.
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Immunological Techniques
OBJECTIVES By the end of this topic, the trainee should be able to: 1.Define terms. 2.Describe types of immunity. 3.Describe types of immune cells. 4.Describe the lymphoid organs and tissues. 5.Describe serological and immunological techniques.
0/8
Herbarium Techniques
OBJECTIVES By the end of this topic , the trainee should be able to: 1.Explain terms 2.Describe importance of collecting and preserving herbarium specimens 3.Describe sources of herbarium specimens 4.Describe collection of herbarium specimens 5.Describe preservation of herbarium specimens 6.Describe display of herbarium specimens
0/8
Museum Techniques
OBJECTIVES By the end of this topic, the trainee should be able to: 1.Explain terms. 2.Describe importance of collecting and preserving museum specimens. 3.Describe sources of museum specimens. 4.Describe collection of museum specimens. 5.Describe preservation of museum specimens. 6.Describe display of museum specimens
0/5
Vivarium Techniques
OBJECTIVES By the end of this topic, the trainee should be able to: 1.Explain terms. 2.Describe importance of vivarium. 3.Describe essential features of a vivarium. 4.Describe construction of a vivarium. 5.Describe maintenance of a vivarium.
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Aquarium Techniques
OBJECTIVES By the end of this topic, the trainee should be able to: 1.Explain terms. 2.Describe importance of aquariums. 3.Describe essential features of an aquarium tank. 4.Describe construction of an aquarium tank. 5.Describe maintenance of an aquarium tank.
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Laboratory Animals
OBJECTIVES The objective of this chapter is to give a better understanding of the technical requirements regarding handling, care and maintained of various laboratory animals In this chapter, we will; 1. Identify the various types of laboratory animals. 2.Discuss the general care and handling of laboratory animals. 3. Describe the various methods of restraining and humane killing laboratory animals 4.Discuss care of specific disease free (SPF)and Gnotobiotic animals
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Introduction to Ecology
OBJECTIVE By the end of this module, the trainee should be able to: 1.Explain terms. 2.Describe biotic and abiotic factors. 3.Explain adaptation of organisms to terrestrial and aquatic environment. 4.Describe the energy flow in ecosystem. 5.Explain estimation of population in ecosystem. 6.Describe influence of human activities on environment. 7.Describe basic biogeochemical cycles.
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Plant Anatomy and Physiology
OBJECTIVES By the end of this topic, the trainee should be able to: 1.Describe of plant parts and tissues. 2.Describe functions of various plant tissues. 3.Describe processes in plants .
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Biology Techniques For Science Laboratory Technicians
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Protein Denaturation 

Protein denaturation refers to the process in which a protein loses its structural and functional integrity, resulting in the disruption or unfolding of its native three-dimensional structure. Denaturation can occur due to various factors such as heat, pH changes, exposure to chemicals, mechanical agitation, or high concentrations of denaturing agents.

 During denaturation, the protein’s secondary, tertiary, and sometimes quaternary structures are disrupted, while the primary structure (amino acid sequence) remains intact. The protein may unfold into a random coil or adopt alternative conformations.

 The native structure of a protein is stabilized by a variety of non-covalent interactions, including hydrogen bonds, electrostatic interactions, van der Waals forces, and hydrophobic interactions. Denaturation disrupts these interactions, leading to loss of protein structure.

 Denaturation often results in the loss of protein function. The functional properties of proteins, such as enzymatic activity or binding ability, depend on their specific three-dimensional structure. When denaturation occurs, the protein may no longer be able to perform its normal biological functions.

Factors Causing Denaturation:

  1. Heat: Elevated temperatures can disrupt the weak bonds that hold the protein structure together, causing denaturation. The specific temperature at which denaturation occurs varies for each protein.
  2. pH Changes: Extreme pH values (high or low) can alter the charges on amino acid residues, affecting the protein’s folding and stability.
  3. Chemicals: Certain chemicals, such as urea or guanidine hydrochloride, can disrupt non-covalent interactions and denature proteins. Organic solvents and heavy metals can also cause denaturation.
  4. Mechanical Agitation: Physical forces, such as stirring, shaking, or sonication, can disrupt the protein structure and lead to denaturation.

Renaturation: In some cases, denatured proteins can regain their native structure and function under appropriate conditions. This process is called renaturation or refolding. Renaturation involves the gradual removal of denaturing conditions and allowing the protein to refold correctly. However, not all denatured proteins can be renatured successfully.

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