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proteins

TermDefinition
What elements make up proteins? Carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur.
Define amino acid. The monomer of proteins containing an amino group, a carboxyl group, a hydrogen atom, and an R group.
What determines the properties of an amino acid? The R group (side chain).
How many amino acids are used to build proteins? Twenty standard amino acids.
Define dipeptide. A molecule formed when two amino acids are joined by a peptide bond.
Define polypeptide. A long chain of amino acids linked by peptide bonds.
What reaction links amino acids together? Condensation reaction that releases water.
What bond forms between amino acids? Peptide bond.
Where are polypeptides synthesized? On ribosomes during translation.
What determines the sequence of amino acids in a protein? The gene that codes for the protein.
Define primary structure. The linear sequence of amino acids in a polypeptide chain.
Define secondary structure. Folding of the polypeptide into alpha helices or beta-pleated sheets through hydrogen bonding.
Define tertiary structure. The overall three-dimensional shape of a polypeptide formed by interactions between R groups.
Define quaternary structure. The association of multiple polypeptide chains to form a functional protein.
Examples of quaternary proteins. Hemoglobin and collagen.
What interactions stabilize tertiary structure? Hydrogen bonds, ionic interactions, hydrophobic interactions, and disulfide bridges.
Define globular protein. A compact, spherical, water-soluble protein with metabolic functions.
Example of globular protein. Enzymes, hemoglobin, antibodies.
Define fibrous protein. A long, insoluble, structural protein with repetitive sequences.
Example of fibrous protein. Collagen, keratin.
Why are fibrous proteins strong? Their long, parallel polypeptide chains form stable fibers through cross-linking.
Why are globular proteins soluble? Hydrophilic R groups are positioned on the outside of the molecule.
Define denaturation. Loss of protein structure and function due to factors like heat or changes in pH.
How does heat cause denaturation? It breaks weak interactions such as hydrogen bonds, altering protein shape.
How does pH cause denaturation? It changes charges on R groups and disrupts ionic bonds.
Can denaturation be reversed? Usually no, because the protein cannot refold into its original shape.
Functions of proteins in organisms. Enzymes, structure, transport, movement, defense, signaling.
Example of structural protein. Collagen in connective tissue.
Example of transport protein. Hemoglobin carrying oxygen.
Example of hormonal protein. Insulin.
Example of defensive protein. Antibodies.
Example of contractile protein. Actin and myosin in muscles.
What is the proteome? The complete set of proteins produced by a cell, tissue, or organism.
Why is the proteome unique to each individual? Different genes are expressed and proteins change with conditions.
Difference between genome and proteome. Genome is all genes; proteome is all expressed proteins.
Why are proteins highly diverse? With 20 amino acids, sequences and folds can form billions of unique structures.
What determines a protein’s final function? Its three-dimensional conformation.
Why is collagen important? It provides tensile strength to skin, tendons, and ligaments.
Why is hemoglobin important? It binds and transports oxygen in red blood cells.
What are conjugated proteins? Proteins that contain a non-protein component (prosthetic group).
Example of protein with prosthetic group. Hemoglobin contains a heme group.
What are prions? Misfolded proteins that cause disease by inducing misfolding in other normal proteins.
Created by: user-1970252
 

 



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