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Define: Acidic amino acid
An amino acid that has an R group with a carboxylate (COO-) ion.
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What is a secondary level of protein structure, in which hydrogen bonds connect the N-H of one peptide bond with C=O of a peptide bond farther down the chain to form a coiled or corkscrew structure?
alpha helix
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Define: alpha keratins
Fibrous proteins containing mostly alpha helices found in hair, nails, and skin.
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What is the building block of proteins, consisting of an ammonium group, a carboxylate group, and a unique R group attached to the alpha carbon?
Amino acids
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Define: Basic amino acid
An amion acid that contains an R group with an ammonium (NH3+) ion.
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What is a secondary level of protein structure that consists of hydrogen bonds between peptide links in parallel polypeptide chains?
beta-pleated sheet
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Define: C terminal
The end amion acid in a peptide chain with a free carboxylate (COO-) group.
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What is the most abundant form of protein in the body, which is composed of fibrils of triple helics with hydrogen bonding between -OH groups of hydroproline and hydroxylysine?
Collagen
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Define: denaturation
the loss of secondary and tertiary protein structure caused by heat, acids, bases, organic compounds, heavy metals, and/or agitation.
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What is the covalent S-S bonds that form between the -SH groups of two cysteines in a protein to stabilize the tertiary struture?
Disulfide bonds
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Define: electrophoresis
the use of electrical current to separate proteins or other charged molecules with different isoelectric points
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What are amino acids that must be supplied by the diet because they are not synthesized by the body?
essential amion acids
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Define: Fibrous proteins
Proteins that are insoluble in water, consisting of polypeptide chains with alpha helices or beta-pleated sheets, and comprising the fibers of hair, wool, skin, nails, and silk.
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What are proteins that acquire a compact shapte from attractions between the R groups of the amino acids in the protein?
Globular proteins
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Define: Hydrogen bonds
the interactions between water and te polar R groups such as -OH, -NH2, and -COOH on the outside surface of a polypeptide chain.
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What is the attraction between polar R groups on the protein surface and water?
Hydrophilic interactions
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Define: Hydrophobic interactions
the attractions between nonpolar R groups on the inside of a globular protein
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What is the pH at which an amino acid exists as a zqitterion with a net charge of zero?
isoelectric point (pI)
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Define: N terminal
the end amino acid in a peptide with a free NH3+ group.
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What are amino acids with nonpolar R groups containing only C and H atoms?
Nonpolar amino acids
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Define: peptide
the combination of two or more amino acis joined by pepide bonds; dipeptide, tripeptide, and so on.
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What is the amide bond in peptides that joins the carboxylate group of one amion acid with the ammonium group in the next amino acid?
peptide bonds
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Define:Polar amino acids (neutral)
amino acids with polar R groups
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What is the specific sequence of the amino acids in protien?
primary structure
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Define: Protein
polypeptides containing many amino acids linked together by peptide bonds that are biologically active.
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What are protein structures in which two or more protin subunits form an active protein?
Quaternary structure
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Define: Salt bridge
the attraction between the ionized R groups of basic and acidic amion acids in the tertiary structure of a protein.
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Define: Secondary struture
the formation of an alpha helix, beta-pleated sheet, or triple helix
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What is the folding of the secondary structure of a protein into a compact structure that is stabilized by the interactions of R groups such as ionic and disulfide bonds?
tertiary struture
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Define: Triple Helix
the protein structure found in collagen consisting of three polypeptide chains woven together like a braid
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What is the dipolar form of an amino acid consisting of two oppositely charged ionic regions, NH3+ and COO-?
Zwitterion
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List each of the 7 classes of proteins and give its function in the body and an example of each.
1) STRUCTURAL - provide structure; i.e. collagen & keratin, 2) CONTRACTILE - move muscles; i.e. myosin, 3) TRANSPORT - Carry essential substances through the body; i.e. Hemoglobin & Lipoproteins, 4) STORAGE - Store nutrients; i.e. casein, 5) HORMONE- body regulation; i.e. Insulin & Growth Hormone, 6) ENZYME - catalyze biochemical reactions; i.e. sucrase, 7)PROTECTION - destroy foreign bodies; i.e. Immunoglobulins
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What happens to H+ when pH < pI?
increases
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What happens to H+ when pH > pI?
decreases
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