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Macromolecules
Large molecules often made of carbon, hydrogen, nitrogen, oxygen, phosphorous, and sulfur.
Polymers
Large molecules consisting of many identical or similar, connected subunits called monomers.
Monomers
The subunits that make up polymers.
Dehydration Reaction
A chemical reaction that creates a polymer from multiple monomers, producing water.
Hydrolysis Reaction
A chemical reaction that creates many monomers from a polymer.
Carbohydrates
Macromolecules made of chains of monomers called monosaccharides, linked by dehydration reactions.
Monosaccharides
Simple sugars containing carbon, hydrogen, and oxygen in a ratio of C:H2:O.
Energy Storage
A function of carbohydrates, exemplified by starch in plants and glycogen in animals.
Structural Support
A function of carbohydrates, exemplified by cellulose in plants.
Lipids
Diverse macromolecules that are hydrophobic and soluble in special solvents.
Fats (Triglycerides)
Lipids composed of a glycerol head and three fatty-acid chains, used for energy storage.
Phospholipids
Lipids similar to triglycerides but with two fatty acid chains, important for cell membrane structure.
Sterols
Lipids with four fused carbon rings, involved in hormone signaling and cell membrane integrity.
Hydrophobic
A characteristic of lipids, indicating they do not mix with water.
Energy Source
Energy stored in bonds of carbohydrates is used by cells to make ATP.
Polysaccharides
Complex carbohydrates formed by linking monosaccharides together.
Amphipathic
A property of phospholipids indicating they have both hydrophilic and hydrophobic ends.
Functional Diversity
The variation in functions of sterols due to different atoms attached to their structure.
Nutrition
The importance of monosaccharides like glucose for energy in living organisms.
Cell Membrane Components
Lipids play a crucial role in forming the structure of cell membranes.
Hormone Signaling
A function of lipids, particularly sterols, in regulating body fluids and signaling.
Proteins
Macromolecules made of amino acids linked by peptide bonds, sharing a common backbone N-C-C.
Amino acids
Subunits of proteins, approximately 20 in humans.
Peptide Bonds
The special covalent bonds that link amino acids to form a polypeptide chain.
Polypeptide chain
A chain formed by linked amino acids.
Importance of Shape - conformation
3-D Shape (Native Conformation) enables it to work/interact with other molecules and forms as it is assembled.
Self-stabilizing
The ability of a protein to maintain its structure using bonds.
Primary Structure
The actual order of the amino acids of the chain, determined by DNA sequence.
Sickle cell anemia
A condition caused by slight changes in the primary structure of proteins (Glu>Val).
Secondary Structure
Small, regular & repeated foldings and coilings of a protein's backbone, stabilized by H-bonds.
Examples of Secondary Structure
a-helix, b-sheets.
Tertiary Structure
Final bending & folding of the protein due to interactions of side-groups (R) with each other and surrounding water.
Quaternary Structure
The structure assumed between multiple subunits of a protein, occurring only in proteins with multiple subunits (e.g., collagen, hemoglobin).
Nucleic Acids
Molecules of inheritance responsible for information storage.
Nucleotides
Monomers of nucleic acids consisting of sugar, phosphate, and base.
DNA (deoxyribonucleic acid)
Contains coded information for making proteins and controls all of the cell's activities.
Genes
Short DNA sequences coding for a single protein.
RNA (ribonucleic acid)
Functions in making proteins, is single stranded, and has three types: mRNA, tRNA, rRNA.
mRNA
Messenger RNA, a type of RNA involved in protein synthesis.
tRNA
Transfer RNA, a type of RNA that helps in protein synthesis.
rRNA
Ribosomal RNA, a type of RNA that is a component of ribosomes.