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Vocabulary flashcards covering chemical polarity, properties of water, hydrogen bonding, and biomolecules including carbohydrates, lipids, and protein structure/folding.
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Polar Covalent Bond
A type of chemical bond where electrons are shared unequally between atoms, creating partial positive (δ+) and partial negative (δ−) charges on the molecule.
Hydrogen Bond
A weak attraction between a hydrogen atom in a polar covalent bond and another atom (usually oxygen, nitrogen, or sulfur) taking part in a separate polar covalent bond.
Cohesion and Adhesion
Unique characteristics of water driven by hydrogen bonding that allow water molecules to stick to each other and other surfaces, enabling water to move from a plant's roots to its leaves.
Hydrophilic
Refers to 'water-loving' substances, such as charged ions or polar molecules, that readily interact with and dissolve in polar water molecules.
Hydrophobic
Refers to substances that are nonpolar (such as oils composed of carbon and hydrogen) and do not dissolve in or interact with water.
Monomer
A single molecular subunit (mono=one) that serves as the fundamental building block used to construct larger polymer molecules.
Polymer
A large, interlocking molecule (poly=many) built out of repeating monomer subunits, made up mostly of carbon, nitrogen, oxygen, and hydrogen.
Monosaccharide
A single sugar monomer (mono=one), such as Ribose (C5H10O5), Glucose (C6H12O6), or Fructose (C6H12O6).
Disaccharide
A sugar molecule formed by combining two monosaccharides (di=two), such as Sucrose (C12H22O11).
Polysaccharide
A complex carbohydrate polymer (poly=many) composed of many monosaccharide units linked together, such as Cellulose, Starch, and Glycogen.
Lipids
A class of biomolecules composed mostly of nonpolar carbon and hydrogen structures, including triglycerides (chains with saturated or unsaturated fatty acids) and steroids (rings like Testosterone).
Amino Acid
The building block monomer of proteins, consisting of a central carbon, an amino group (containing nitrogen), a carboxyl group, and one of 20 different R groups.
Primary Protein Structure
The linear sequence of a chain of amino acids linked together by strong covalent bonds.
Secondary Protein Structure
The repeating folding pattern of a protein chain, such as an alpha helix or beta-pleated sheet, stabilized by hydrogen bonding along the peptide backbone.
Tertiary Protein Structure
The overall three-dimensional folding pattern of a single protein chain resulting from interactions among the amino acid side chains (R groups).
Quaternary Protein Structure
A protein structure formed when a protein consists of more than one folded amino acid chain (polymer).
Protein Denaturation
The process in which heat or other factors break the hydrogen bonds maintaining a protein's shape and folding (changing color and texture), without breaking the covalent bonds between amino acids.