Bio Exam 1: Ch. 3

Front 1

Loss of a protein's normal 3D shape because of high temperatures or changes in pH is called:

A) metabolism

B) denaturation

C) hydrolysis

D) condensation

Back 1

B) denaturation

Front 2

True or false, and a condensation reaction, small molecules come together to make a large molecule?

Back 2

True

Front 3

Two molecules into one; one molecule is stripped of its H+, another is stripped of its OH- ; then the two molecule fragments join to form a new compound and the H+ and OH- form water.

Back 3

Condensation reaction

Front 4

One molecule into two; what molecule is split by the addition of H+ and OH- (from water) to the components.

Back 4

Clevage hydrolysis

Front 5

True or false, ribose is a six-carbon monosaccharide.

Back 5

False, ribose and deoxyribose have 5 carbon backbones

Front 6

One sugar unit; are the simplest carbohydrates; they are the building blocks of carbohydrates

Back 6

Monosaccharides

Front 7

How many carbon backbones do ribose and deoxyribose have?

Back 7

5

Front 8

How many carbon backbones do glucose and fructose have?

Back 8

6

Front 9

The building blocks of nucleic acids are?

Back 9

Nucleotides

Front 10

The building blocks of proteins are?

Back 10

Amino acids

Front 11

The building blocks of most lipids and glycerol are?

Back 11

Fatty acids

Front 12

The building blocks of carbohydrates are?

Back 12

Monosaccharides

Front 13

A short chain of two or more sugar monomers

Back 13

Oligosaccharide

Front 14

Two sugar units, are the simplest

Back 14

Disaccharides

Front 15

A straight or branched chain of hundreds or thousands of sugar monomers

Back 15

Polysaccharide

Front 16

A plant storage form of energy, arranged as unbranched coiled Chainz, easily hydrolyzed into glucose units

Back 16

Starches; easily broken down

Front 17

A fiberlike structural material-tough. insoluble-used in plant cell walls

Back 17

Cellulose

Front 18

A highly branched chain used by animals to store energy in their muscles and liver

Back 18

Glycogen

Front 19

A specialized polysaccharide with nitrogen attached to its glucose units, it is used in a structural material in anthropod exoskeletons and fungal cell walls

Back 19

Chitin

Front 20

How many kinds of amino acids are available in nature?

Back 20

20

Front 21

Proteins that have polypeptide chains organized as strands or sheets, they contribute to the shape, internal organization, and movement of cells

Back 21

Fibrous proteins

Front 22

Proteins that, including most enzymes, have their chains folded into compact, rounded shapes

Back 22

Globular proteins

Front 23

Ordered sequences of amino acids linked together by peptide bonds to form peptide chains

Back 23

Primary structure

Front 24

The helical coil or sheet-like array that results from hydrogen bonding of side groups on the amino acid chains; the peptide bonds between the amino acids of primary structure allows a slight bending to permit this structure

Back 24

Secondary structure

Front 25

The result of folding due to interactions among R groups along the polypeptide chain; the result is a more compact globular shape in complex proteins

Back 25

Tertiary structure

Front 26

Describes the complexity (chemical bonding) of two or more polypeptide chains

Back 26

Quaternary structure

Front 27

Have both lipid and protein components, they transport fat and cholesterol in blood

Back 27

Lipoproteins

Front 28

Consist of oligosaccharides covalently bonded to proteins, they are abundant on the exterior of animal cells, as cell products, and in the blood

Back 28

Glycoproteins

Front 29

Double-stranded Helix carrying encoded hereditary instructions

Back 29

DNA

Front 30

Single stranded and functions in translating the code to build proteins

Back 30

RNA