Chapter 19- Amino Acids And Proteins Flashcards

1
Q

Acidic amino acid

A

An amino acid has an R group with a carboxylate (-COO) ion

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2
Q

A (alpha) helix

A

A secondary level of protein structure, in which hydrogen bonds connect the N-H of one peptide bond with the ( C=O) of a peptide bond further down the chain to form a coiled or corkscrew structure

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3
Q

A-keratins

A

Fibrous proteins containing mostly a Helixes found in hair,nails, and skin

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4
Q

Amino acids

A

The building block of proteins, consisting of an ammonium group,ma carboxylate group, and a unique R group attached to the a carbon

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5
Q

Basic amino acid

A

An amino acid that contains an R group with an ammonium (-NH3+) ion

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6
Q

B-pleated sheet

A

A secondary level of protein structure that consists of hydrogen bonds between peptide links in parallel polypeptides

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7
Q

C terminal

A

The end amino acid In a peptide chain with a free carboxylate (-COO) group

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8
Q

Collagen

A

The most abundant form of protein in the body, which is composed if fibrils of triple Helixes with hydrogen bonding between the -OH groups ofnhydroxyproline and hydroxylisine

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9
Q

Denaturation

A

The loss of secondary or tertiary protein structure caused by heat, acids, bases, organic compounds, heavy metals, and/or agitation

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10
Q

Disulfide bond

A

Covalent -S-S- bonds that firm between the -SH groups of two cysteines in a protein to stabilize the tertiary structure

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11
Q

Electrophoresis

A

The use of electrical current to separate proteins or other charged molecules with different isoelectric points

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12
Q

Essential amino acids

A

Amino acids that must be supplied by the diet because they are not synthesized by the body

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13
Q

Fibrous proteins

A

Proteins that are insoluble in water; consisting of polypeptide chains with a- Helixes or b-pleated sheets, and comprising with fibers of hair, skin, nails, and silk

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14
Q

Globular proteins

A

Proteins that acquire a compact shape from attractions between the R groups of the amino acids in the protein

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15
Q

Hydrogen bonds

A

The interactions between water and the polar R groups such as -OH, -NH2, and -COOH on the outside surface of polypeptide chain

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16
Q

Hydrophilic reactions

A

The attractions between polar R groups on the protein surface and water

Water attracting

17
Q

Hydrophobic interactions

A

The attractions between non polar R groups on the inside of a globular protein

Water fearing

18
Q

Isoelectric point (pI)

A

The pH at which amino acid exists as a zwitterion with a net charge of zero

19
Q

N terminal

A

The end amino acid in a peptide with a free -NH3+ group

20
Q

Nonpolar amino acids

A

Amino acids with Nonpolar R groups containing only C and H atoms

21
Q

Peptide

A

The combination of two or more amino acids joined by peptide bonds; di peptide, tripeptide, and so on

22
Q

Polar amino acids (neutral)

A

Amino acids with polar R groups

23
Q

Primary structure

A

The specific sequence of the amino acids in a protein

24
Q

Protein

A

Polypeptides containing many amino acids linked together by peptide bonds that are biologically active

25
Q

Quaternary structure

A

A protein structure in which two or more protein subunits form an active protein

26
Q

Salt bridge

A

The attraction between the ionized R groups of basic and acidic amino acids in the tertiary structure of a protein

27
Q

Secondary structure

A

The formation of an a-helix, b-pleated sheet, or triple helix

28
Q

Tertiary structure

A

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

29
Q

Triple helix

A

The protein structure found in collagen consisting of three polypeptide chains woven together like a braid

30
Q

Zwitterion

A

The diplomat form of an amino acid consisting of two oppositely charged ionic regions, -NH3+, and -COO