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Reviewer for Chemistry for grade 12 students
Typology: Lecture notes
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PROTEI NS most abundant organic molecules in living systems
a biological macromolec ule
TYPE EXAMPLES FUNCTIONS Digestive Enzymes Amylase, Lipase, Pepsin, Trypsin Helps in digestion of food by catabolizing nutrients into monomeric units Transport Hemoglobin, Albumin Carry substances in the blood or lymph throughout the body Structural Actin, Tubulin, Keratin Construct different structures like the cytoskeleton Hormones Insulin, Thyroxine Coordinate the activity of different body systems Defense Immunoglobulins Protect the body from foreign pathogens Contractile Actin, Myosin Affect muscle contraction Storage Legume storage proteins, Egg white (Albumin) Provide nourishment in early development of the embryo and the seedling
FACTORS AFFECTING ENZYME ACTIVITY Substrate concentration The enzyme activity increases as the concentration increases but after it has reached the point of saturation, the enzyme activity stays constant. pH Enzyme activity increases when pH level also increases, but after reaching optimum pH, the enzyme starts to denature.
Enzyme activity increases when temperature also increases, but denatures after it has reached its optimum temperature.
There are 20 amino acids present in the proteins. The amino acid’s chemical nature is determined by its R group or its side chain. It could be acidic, basic, polar or nonpolar.
PROTEIN STRUCTURE PRIMARY STRUCTURE polypeptide chain SECONDARY STRUCTURE Hydrogen bonds are the backbones of α- helix and β- pleated sheets TERTIARY^ protein structure STRUCTURE 3D folding pattern due to side chain interactions QUARTERNAR Y STRUCTURE (Optional) Protein consisting of more than one polypeptide
DENATURATION May be reversible or irreversible Protein loses is shape and function if subjected to temperature, pH and chemical changes.