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Define: Monomer

A molecule that can be bonded to other identical molecules to form a polymer.

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Define: Monomer

A molecule that can be bonded to other identical molecules to form a polymer.

Define: Polymer

A substance or material consisting of very large molecules, or macromolecules, composed of many repeating subunits.

Define: Nucleic Acid

A polymer consisting of nucleotide monomers; the blueprint for proteins and all cellular activities. DNA and RNA are examples.

Define: Protein

A biologically functional molecule consisting of one or more polypeptides folded and coiled into a specific three-dimensional structure.

Define: Carbohydrate

A sugar (monosaccharide) or one of its dimers (disaccharides) or polymers (polysaccharides).

Define: Lipid

Any of a group of large biological molecules, including fats, phospholipids, and steroids, that are insoluble in water.

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.