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Flashcards covering protein structure (primary to quaternary), amino acid structure, peptide bonds, polypeptides, folding in water, and enzyme function.
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What is the primary protein structure?
A chain of amino acids.
What is the secondary protein structure?
Amino acid sequences linked by hydrogen bonds (forming structures like alpha helices and beta pleated sheets).
What is the tertiary protein structure?
Overall 3D shape arising from attractions/interactions between R groups and other parts of the polypeptide, including interactions between alpha helices and beta sheets.
What is the quaternary protein structure?
A protein consisting of more than one amino acid chain (polypeptide).
What is a monomer in a protein?
The small unit of a protein; a single amino acid.
What is a polymer in the context of proteins?
A large unit made of many amino acids; in proteins this is a polypeptide chain.
What groups are attached to the alpha carbon of an amino acid?
An amino group (-NH2), a carboxyl group (-COOH), a hydrogen, and an R group (side chain).
What is the R group in an amino acid?
The side chain that gives each amino acid its unique properties.
What are peptide bonds?
Covalent bonds that link amino acids together to form a polypeptide chain.
When do peptide bonds form?
When the carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH2) of another.
What is another name for a protein?
Polypeptides.
What is a beta sheet?
Hydrogen bonds between carbonyl groups in one polypeptide and amide groups in a different part of the polypeptide.
What causes the tertiary structure of a protein?
Interactions involving the R group (side chains).
How do proteins fold in water?
Nonpolar parts fold inward (to the interior) and polar parts stay on the exterior, making the exterior polar.
What are enzymes?
Proteins that accelerate chemical reactions, making them happen more quickly.
Where must a substrate bind on an enzyme?
The active site.
What happens to enzymes when the temperature is too high?
They denature.