Chemistry Ii - 19.5; Protein Structure: Tertiary And Quarternary Levels

Front 1

When a protein contains amino acid residues who interact and repell one another, what is the structure of the protein likely to be?

Back 1

A tertiary structure

Front 2

What brand of interactions are hydrophilic interactions, hydrophobic interactions, salt bridges, hydrogen bonds, and disulfide bonds?

Back 2

Stabilizing interactions of tertiary structures

Front 3

What interactions have an external aqueous environment pull the polar amino acid residues of a protein to the outer surface?

Back 3

Hydrophilic interactions

Front 4

What interactions have nonpolar amino acid residues form nonpolar centers inside the protein?

Back 4

Hydrophobic interactions

Front 5

What interactions have ionic attractions between the acidic and basic residues of amino acid residues?

Back 5

Salt bridges

Front 6

What interactions form between the hydrogen atom of a polar residue and the oxygen or nitrogen atom of a second polar amino acid residue?

Back 6

Hydrogen bonds

Front 7

What interactions have covalent bonds between the —SH groups of two cysteine residues?

Back 7

Disulfide bonds

Front 8

What to the names primary, α-helix, β-pleated sheet, and triple helix indicate?

Back 8

Protein structures

Front 9

What protein structure consists of polypeptide chains held side-by-side by H bonds?

Back 9

β-pleated sheet

Front 10

What protein structure consists of a sequence of amino acids in a polypeptide chain?

Back 10

Primary structure

Front 11

What protein structure consists of a corkscrew shape with H bonds between amino acids?

Back 11

α-helix

Front 12

What protein structure consists of three peptide chains woven like a rope?

Back 12

Triple helix

Front 13

What's the name of a protein who's spherical shape forms when polypeptide chains fold over each other?

Back 13

Globular proteins

Front 14

What proteins are responsible for the work of cells?

Back 14

Globular proteins

Front 15

What proteins consist of long, thin, fiber-like shapes and are involved in the structure of cells and tissues?

Back 15

Fibrous proteins

Front 16

What do α-kerotins and β-kerotins have in common?

Back 16

They are both kinds of fibrous proteins

Front 17

What type of fibrous protein contains three α-helices linked by disulfide bonds?

Back 17

α-keratins

Front 18

What kind of fibrous protein contains a large amount of a β-pleated sheet structure?

Back 18

β-keratin

Front 19

What's the name of the structure that features two or more polypeptide chains or subunits?

Back 19

Quarternary structures

Front 20

What protein consists of two α-chains with 141 amino acids and two β-chains with 146 amino acids?

Back 20

Hemoglobin

Front 21

What is the bodily function of hemoglobin?

Back 21

Transportation of oxygen in blood

Front 22

What brand of stabilizing interactions are the interactions of hemoglobin identical to?

Back 22

Tertiary interactions

Front 23

The subunits of hemoglobin consist of globular proteins. What is the name of the functional group that each of these subunits contain, capable of binding to an O molecule?

Back 23

Heme group

Front 24

Hemoglobin and myoglobin both carry oxygen, but where does myoglobin carry oxygen in?

Back 24

In the muscles

Front 25

Of hemoglobin and myoglobin, which one has a molar mass of 17,000 and 67,000?

Back 25

Myoglobin; hemoglobin

Front 26

What structural levels do proteins often consist of?

Back 26

Primary, secondary, tertiary, and quarternary; all four