Proteins

Question 1

What are the many functions of proteins

Answer 1

Serve as catalysts (enzymes) in metabolic reactions
Act in defense 
Aid in transport
Contribute to structural support
Cause movement
Perform regulation
Provide storage

Question 2

what is the general structure of proteins

Answer 2

one or more strands of amino acid monomers

Question 3

How many amino acids are there

Answer 3

20

Question 4

Each protein has an

Answer 4

amine and a carboxyl functional group( both are covalently linked to same carbon atom)

Question 5

The carbon is also covalently bonded to

Answer 5

a hydrogen and different side chain structures

Question 6

Amino acids are covalently linked

Answer 6

by peptide bonds

Question 7

strand of amino acid are

Answer 7

oligopeptide,polypeptide and protein

Question 8

number of amino acids in a oligopeptide

Answer 8

3-20

Question 9

number of amino acids in a polypeptide

Answer 9

21-199

Question 10

number of amino acids in a protein

Answer 10

200+

Question 11

Glycoproteins are

Answer 11

proteins with a carbohydrate attached

Question 12

what are the categories of amino acids

Answer 12

nonpolar, polar, charged, special

Question 13

Nonpolar amino acids

Answer 13

contain R groups with hydrogen or hydrocarbons

group with other nonpolar amino acids by hydrophobic interactions

Question 14

Polar amino acids

Answer 14

Contain R groups with other elements besides hydrogen or hydrocarbons
Form interactions with other polar amino acids and with water

Question 15

charged amino acids

Answer 15

Contain R groups with a negative or a positive charge
Form ionic bonds between negatively and positively charged amino acids
Hydrophilic

Question 16

amino acids with special functions

Answer 16

Contain R groups with a negative or a positive charge
Form ionic bonds between negatively and positively charged amino acids
Hydrophilic

Question 17

The structures of amino acids are

Answer 17

primary, secondary, tertiary, quaternary,

Question 18

Primary structure

Answer 18

linear sequence of amino acids

Question 19

Confromation is

Answer 19

three-dimensional shape of the protein
(Crucial for protein function
Levels of organization beyond primary structure
Arrangements dependent upon intramolecular attractions between amino acids
Obtained through folding with help of specialized proteins, chaperones)

Question 20

Intramolecular interactions

Answer 20

Hydrophobic interactions with nonpolar amino acids farther from water
Hydrogen bonds between polar R groups, between amine and carboxylic acid groups
Ionic bonds between negative and positive R groups
Disulfide bonds between cysteine amino acids

Question 21

secondary structures

Answer 21

Patterns that may repeat several times
Confer unique characteristics
Two types

Question 22

two types of secondary structures

Answer 22

alpha helix(spiral coil) and beta sheet(planar pleat arrangement)

Question 23

Tertiary structure is

Answer 23

Three-dimensional shape of poly-peptide chain

Question 24

2 categoreis of tertiary structure is

Answer 24

Globular proteins fold into compact shape

Fibrous proteins are extended linear molecules

Question 25

Quaternary structure is

Answer 25

Present in proteins with two or more polypeptide chains

E.g., hemoglobin with its four polypeptide chains

Question 26

Prosthetic groups

Answer 26

Nonprotein structures covalently bonded to protein

Question 27

Denaturation

Answer 27

Conformational change to a protein
Disturbs protein activity
Usually irreversible
May occur due to increased temperature or in response to changes in pH