3.2 proteins Flashcards

1
Q

proteins

A

polymers made up of amino acids

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2
Q

polypeptide chain

A

unbranched polymers of covalently linked amino acids

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3
Q

structure of Amino Acid

A

carboxyl group, amino group, central carbon, side chain and hydrogen

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4
Q

disulfide bridge

A

two cysteine molecules in a polypeptide chain form by removal of H. determines how a polypeptide chain folds

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5
Q

peptide linkage

A

joins amino acid monomers together. carboxyl group of one amino acid reacts with one amino acid, undergoing condensation. peptide bond carry partial charges that favors hydrogen bond

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6
Q

primary structure

A

Amino acid monomers are joined by peptide bonds forming polypeptide chain

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7
Q

secondary structure

A

polypeptide chains may form alpha helix or beta pleated sheets through hydrogen bonds

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8
Q

Tertiary

A

Polypeptides fold, forming specific shapes. stabilized by disulfide bridges, hydrogen bonds and hydrophobic interactions

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9
Q

quaternary

A

two or more polypeptide assemble to form larger protein molecules. stabilized by hydrogen bond, disulfide bridge, ionic and hydrophobic interactions.

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10
Q

Denatured

A

the disruption of secondary and tertiary due to moderate heat

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11
Q

covalent modification

A

modification of protein structure by the covalent bonding of a chemical group to the side chain of an amino acid

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12
Q

chaperones

A

special class of proteins that protect the 3-D structures by surrounding new or denatured proteins and prevent them from binding to the wrong substance.

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