Lecture 2 Feb 10

Question 1

What is the monomer of a protein?

Answer 1

Amino Acids

Question 2

What is the polymer?

Answer 2

Polypeptide

Question 3

What is the covalent bond for proteins?

Answer 3

Peptides

Question 4

What are amino acids?

Answer 4

They are organic molecules with amino and carboxyl groups

Question 5

What causes amino acids to differ?

Answer 5

R group side chains

Question 6

How many amino acids are there?

Answer 6

20 total

Question 7

Basic Amino acids have what charge?

Answer 7

Positive charge

Question 8

Acidic Amino acids have what charge?

Answer 8

Negative charge

Question 9

What is the key component of non polar side chains?

Answer 9

Hydrocarbon structure/bonds

Question 10

What is key component of polar side chains?

Answer 10

Most contain oxygen or more electronegative molecules

Question 11

What is range in length of polypeptides?

Answer 11

few to >1000; each have unique linear sequence of amino acids

Question 12

What are the four levels of protein structure?

Answer 12

Primary, secondary, tertiary, quaternary

Question 13

What is a primary structure of proteins?

Answer 13

unique sequence of amino acids (polypeptide chain)

Question 14

What is a secondary structure of proteins?

Answer 14

coils and folds in polypeptide chain; result of hydrogen bonds on repeating constituents on backbone

Question 15

What is tertiary structure of proteins?

Answer 15

determined by interactions among various side chains; overall shape of polypeptide is caused by these interactions

Question 16

What is Quaternary structure of proteins?

Answer 16

overall protein structure consisting of multiple polypeptide chains

Question 17

What is an alpha helix?

Answer 17

H bond every 4th peptide bond
* Very common in proteins across membranes

Question 18

What is a Beta Pleated sheet?

Answer 18

typically 3-10 amino acids, need two or more strands, parallel or anti-parallel

Question 19

What is an ionic?

Answer 19

Attraction between cation and anion; acidic/basic R groups

Question 20

What are Van Der Waals interactions?

Answer 20

attractions between molecules that are close together as result uneven distribution in molecule

Question 21

What is a di-sulfide bridge?

Answer 21

Covalent bonds between cysteine, stabilize protein structure by being close together at the bending of the protein

Question 22

Examples of physical and chemical conditions impacting protein structure

Answer 22

pH, salt concentration, temperature, solvent

Question 23

Examples of changing primary structure

Answer 23

Change in primary structure can affect protein’s structure→function

Question 24

What is sickle cell disease?

Answer 24

ONE aa substitution in hemoglobin in the 6th slot in chain
Abnormal hemoglobin cause RBCs to aggregate into chains and deform into a sickle shape; this shape can clog blood vessels and impede blood flow

Question 25

The aa sequence determines protein’s 3D structure
A protein’s structure determines how it works
The function of protein usually depends on
its ability to recognize and bind to some other molecule

Answer 25

The aa sequence determines protein’s 3D structure
A protein’s structure determines how it works
The function of protein usually depends on
its ability to recognize and bind to some other molecule

Question 26

What is the term for when weak chemical bonds are destroyed causing the protein to unravel and lose its shape?

Answer 26

Denaturation

Question 27

When two amino acids are positioned so that the amino group is adjacent to the carboxyl group, they can be joined by what reaction? What type of covalent bond is created?

Answer 27

Dehydration; peptide bond

Question 28

T/F: misfolding of proteins causes many diseases such as Alzheimer’s, Parkinson, and cancer

Answer 28

True