Chapter 3 Questions

Front 1

What are 2 functional groups are present on every amino acid?

Back 1

An amino group and a carboxyl group

Front 2

Twenty different amino acids are found in the proteins of cells. What distinguishes these molecules?

Back 2

The atoms and functional groups found in the side chains.

Front 3

By convention, biologists write the sequence of amino acid in a polypeptide in which direction?

Back 3

Amino- to carboxyl-terminus

Front 4

In a polypeptide, what bonds are responsible for the secondary structure called an X-helix?

Back 4

Hydrogen bonds that form between the core C=O and N-H groups on differ residues.

Front 5

Where is the information stored that directs different polypeptides to fold into different shapes?

Back 5

The order and the type of amino acid (i.e., the primary-structure) contains the information that directs folding.

Front 6

What is an active site?

Back 6

The position in an enzyme where substrates bind

Front 7

Why are proteins not considered to be a good candidate for the first living molecule?

Back 7

They cannot serve as a template for replication.

Front 8

Proteins that interact with DNA often interact with the phosphate that are part of this molecules. Which of the following types of amino acid would you predict to be present in the DNA binding sites of these proteins?

Back 8

Basic amino acids

Front 9

3.1 Amino acid and their polymerization

Back 9

Amino acids have a central carbon bonded to an amino group, a hydrogen atom, a carboxyl group, and an R-group.

Front 10

3.1 Amino acid and their polymerization

Back 10

The structure of the R-group affects the chemical reactivity and solubility of the amino acid.

Front 11

3.1 Amino acid and their polymerization

Back 11

In proteins, amino acids are joined by a peptide bond between the carboxyl group of one amino acid and the amino group of another amino acid.

Front 12

3.2 What do proteins look like?

Back 12

A protein's primary structure, or sequence of amino acid, is responsible for most of its chemical properties.

Front 13

3.2 What do proteins look like?

Back 13

Interactions that take place between C=O and N-H groups in the same peptide-bonded backbone create secondary structures, which are stabilized primarily by hydrogen bonding.

Front 14

3.2 What do proteins look like?

Back 14

Tertiary structure results from interactions between R-groups-R groups and the peptide-bonded backbone- that stabilize a folded protein into a characteristic overall shape.

Front 15

3.2 What do protein look like?

Back 15

In many cases, a complete protein consist of several different polypeptides, bonded together, The combination of polypeptides represents the protein's quaternary structure.

Front 16

3.3 Folding & function

Back 16

Protein folding is a spontaneous process.

Front 17

3.3 Folding & function

Back 17

A Protein's normal shape is essential to its function.

Front 18

3.3 Folding & function

Back 18

Many proteins must first bind to other molecules or ions before they can adopt their active conformation.

Front 19

3.3 Folding & function

Back 19

Improperly folded proteins can be detrimental to life, and certain proteins even cause deadly infectious diseases.

Front 20

3.4 Proteins are the most versatile macromolecules in cells

Back 20

In organisms, proteins function n catalysis, defense, movement, signaling, structural support, and transport of materials.

Front 21

3.4 Proteins are the most versatile macromolecules in cells

Back 21

Proteins can have diverse functions in cells because hey have such diverse structures and chemical properties,

Front 22

3.4 Proteins are the most versatile macromolecules in cells

Back 22

Catalysis takes place at the enzyme's active site, which has unique chemical properties and distinctive size and shape.