All Flashcards
Describe the process of protein denaturation.
Loss of a protein's native structure. This can be caused by changes in pH, salt concentration, temperature, or other factors. Denaturation leads to the protein becoming biologically inactive.
Describe nucleic acid polymerization.
New nucleotides are added to the 3' end of the growing strand, forming a phosphodiester bond between the phosphate group of the new nucleotide and the 3' hydroxyl of the existing nucleotide.
Describe the formation of a peptide bond.
Peptide bonds are formed between amino acids via dehydration synthesis, where a water molecule is removed.
Describe the formation of a glycosidic bond.
Glycosidic bonds are formed between two monosaccharides via dehydration synthesis, where a water molecule is removed.
Compare and contrast starch and cellulose.
Both are polysaccharides found in plants, composed of glucose monomers. Starch is used for energy storage and has alpha linkages. Cellulose is used for structural support (cell walls) and has beta linkages.
Compare and contrast DNA and RNA.
DNA: Double-stranded, deoxyribose sugar, thymine base, stores genetic information. RNA: Single-stranded, ribose sugar, uracil base, carries out instructions from DNA.
Compare and contrast denaturation and hydrolysis.
Denaturation: Loss of protein's 3D structure, but peptide bonds remain intact. Hydrolysis: Breaking of bonds (e.g., peptide or glycosidic) through the addition of water.
What is the effect of a single amino acid change in a protein's primary structure?
It can alter the folding of the protein, leading to changes in secondary, tertiary, and quaternary structures, which can affect the protein's function. Example: Sickle cell anemia.
What is the effect of high temperature on a protein?
High temperature can cause a protein to denature, losing its 3D structure and function.
What is the effect of changing the pH of a solution on a protein?
Changes in pH can disrupt the interactions between R-groups, causing the protein to denature and lose its function.