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What is a proteome?
The entire set of proteins expressed by the genome, allowing organisms to express their phenotypes (characteristics).
What is the monomer of a protein / polypeptide?
Amino acids.
What are the three parts of an amino acid?
Amino group, carboxyl group, and variable side chain (R).
What part of the amino acid makes them structurally different from each other?
R groups.
What is a proteome?
The entire set of proteins expressed by the genome, allowing organisms to express their phenotypes (characteristics).
What is the monomer of a protein / polypeptide?
Amino acids.
What are the three parts of an amino acid?
Amino group, carboxyl group, and variable side chain (R).
What part of the amino acid makes them structurally different from each other?
R groups.
What type of R groups are seen in polar amino acids?
Hydrophilic R groups create polar amino acids.
What type of R groups are seen in nonpolar amino acids?
Hydrophobic R groups create nonpolar amino acids.
How many different amino acids are there?
What are essential amino acids?
Amino acids that the body cannot make and must be present in the diet.
What are non-essential amino acids?
Amino acids produced by the body; not required to be a part of the diet.
What are conditional amino acids?
Amino acids produced by the body, sometimes not enough depending on conditions like pregnancy.
What determines the sequence of amino acids in a polypeptide?
Anabolic/Condensation reactions.
Where does protein synthesis occur in a cell?
In the ribosomes.
How do monomers create dipeptides or polypeptides?
Amino acids bond together, creating dipeptides and polypeptides.
How is a dipeptide or polypeptide broken down into its monomers?
1 water molecule is used to break each peptide bond.
What is the function of Lysozyme?
An enzyme in tears and saliva that breaks down cell walls of bacteria.
What is the function of alpha neurotoxins?
Found in snake venom, disrupts the nervous system.
What is the function of glucagon?
A hormone that raises blood sugar levels.
What is the function of myoglobin?
Stores oxygen for muscles.
Describe denaturation in a protein.
Denaturation occurs when the protein's optimal temperature and pH are exceeded, breaking hydrogen bonds and causing the protein to become biologically ineffective.
What is the primary structure of a protein?
The sequence of amino acids that influences all remaining levels.
What is the secondary structure of a protein?
Folding into alpha helix, beta-pleated sheet, or random coil due to hydrogen bonding between amino and carboxyl groups.
What is the tertiary structure of a protein?
Folding into a complex 3D shape influenced by interactions between R groups.
What is the quaternary structure of a protein?
Multiple polypeptides interacting to form a large, single protein.
What are conjugated proteins?
Proteins that consist of multiple polypeptide chains and have a nonprotein component.
What are non-conjugated proteins?
Proteins that consist of just multiple polypeptide chains.
What are fibrous proteins?
Thin and thread-like proteins that often play structural roles, such as collagen.
What are globular proteins?
Spherical proteins that play active roles in metabolism, such as insulin.
What is an enzyme?
A biological catalyst that is a globular protein, increasing the rate of reaction and lowering activation energy.
What is activation energy?
The amount of energy needed to initiate a reaction.
What is a substrate?
The molecule that interacts with an enzyme, connecting to the enzyme's active site.
What happens to the substrate in a reaction catalyzed by an enzyme?
The substrate is transformed into products and disappears after the reaction.
What are the effects of temperature on enzyme activity?
Low temperatures lead to low activity, optimal temperature peaks activity, and high temperatures can denature the enzyme.
What are the effects of pH on enzyme activity?
Extreme pH can denature enzymes, while optimal pH peaks activity.
How does substrate concentration affect enzyme activity?
Increasing substrate concentration increases activity up to a saturation point (Vmax).
What is end product inhibition?
A mechanism that controls metabolic pathways by where the final product inhibits an earlier enzyme to prevent overproduction.