Lecture 2

Question 1

3 Attributes Necessary For Life

Answer 1

Infromation, Replication and Storage(IRS)

Question 2

Parts of an Amino acids

Answer 2

Amino group on one side, carbon in the middle, Carbonyl group on the other side, side chain at the bottom, and H atom at the top

Question 3

What groups are side chains divided into

Answer 3

Polar, Nonpolar, acidic, and basic

Question 4

What’s another name for a side chain

Answer 4

R group

Question 5

Whats another name for amino acids

Answer 5

Residues

Question 6

How is the solubility of a protein affected by its chemical properties

Answer 6

If the amino acid is charged or polar its hydrophilic and dissolves in water, it the amino acid is uncharged and nonppolar its hydrophobic

Question 7

How to determine if a an amino acid is polar, nonpolar, acidic, or basic.

Answer 7

1. It it is negatively charged, its acidic
2. If it is positively charged, its basic
3. It it is a neutral charge and it has an oxygen atom its polar
4. If it has none of these its nonpolar

Question 8

Where do you look to determine either something is polar, nonpolar, acidic or baisc

Answer 8

Its R group

Question 9

peptide bonds

Answer 9

These are created when bonds form between a carbonyl group of one amino acid, and amino group of another

Question 10

what does polymerize mean?

Answer 10

It means to be created

Question 11

How does a peptide bond form

Answer 11

It forms through a condensation reaction

Question 12

What is a condensation reaction?

Answer 12

water is formed

Question 13

What is a polymer

Answer 13

Its like what the molecules come together to make

Question 14

what is the polymer of amino acids

Answer 14

Protein

Question 15

how many types of structures are there in proteins and what are they

Answer 15

Their are 4 types of structures, and these structures are primary, secondary, and tertiary structure.

Question 16

Primary structure

Answer 16

The sequence of the amino acids

Question 17

How are the R groups oriented in the primary structure

Answer 17

the R groups stick out of the peptide backbone and interact with each other or water.

Question 18

What is the Directionality of the sequences

Answer 18

it has ends with N terminus( free amino group) and C Terminus (free carbonyl group) and it usually written with the N terminus first.

Question 19

What is the flexibilty of the sequences

Answer 19

either terminus can rotate

Question 20

how many amino acid sequences cna be created?

Answer 20

Over 10,000 billion sequences

Question 21

How does the shape and sequence of amino acids affect a protein

Answer 21

What a protein does it determined by the shape and sequence of proteins and one change can have a vast effect.

Question 22

What is secondary structure

Answer 22

The secondary structure is the result of hydrogen bonding and the bonding of one carbonyl group to one of the amino groups

Question 23

What two shapes result from the secondary structure

Answer 23

alpha helix, and beta pleated sheet

Question 24

What does a alpha helix look like

Answer 24

It looks like a spring

Question 25

What doe a beta pleated sheet look like

Answer 25

It looks like two zigzag area's joined together.

Question 26

What is a tertiary structure

Answer 26

It is a structure that develops from the interactions of the side chains causing the peptide backbone to bend and fold, creating important 3 dimensional shapes.

Question 27

How many interactions are there and what are they

Answer 27

There are 5 types of interactions, and they are hydrogen bonding, hydrophobic interactions, Van Der wals interaction, Covalent Bond interaction, and Ionic Bond Interaction

Question 28

What is a hydrogen bonding Interaction

Answer 28

from between polar side chains and opposite partial charges

Question 29

What is a hydrophobic interaction

Answer 29

Water forces between hydrophobic side chains( nonpolar side chains)

Question 30

What is a Van Der Wals interaction?

Answer 30

They are weak electrical interactions between side hydrophobic side chains

Question 31

Oligopeptide

Answer 31

It is a chain of fewer than 50 aminoacids

Question 32

Polypetide

Answer 32

Chains of 50 or more amino acids

Question 33

Covalent bonding Interaction

Answer 33

Covalent bonds bonding between sulfhydryl groups ( Disulfide bonds)

Question 34

Ioninc Bonding interaction

Answer 34

forms between groups with full and opposing charges

Question 35

What is a Quaternary stucture?

Answer 35

Bonding of distinct polypeptides

Question 36

Types of Quaternary Structures:

Answer 36

Dimers, Homedimers, Hetrodimers, Tetramer

Question 37

What is a dimer

Answer 37

When two polypeptide sub units bond together.

Question 38

What is a homodimer?

Answer 38

When the structure consists of two identical subunity

Question 39

What is a heterodimer

Answer 39

When the structure's sub units are not the same

Question 40

What is a Tetramer?

Answer 40

when the structure has 4 polypeptide chains

Question 41

What are moleular chaperones

Answer 41

Molecules that facilitate folding in proteins, they are sesponsible for blocking inappropritate interactions between unfolded proteins

Question 42

How can folding be described?

Answer 42

It is spontaneous, meaning its due to chemical interactions and usually proteins that are folded are more chemically stable than unfolded proteins

Question 43

What is a Denatrued Protein:

Answer 43

Unfolded protein

Question 44

is folding always good.

Answer 44

Altough folding is spontaenous and unfolded proteins dont work properly, folding can be infectious.

Question 45

What are Prions?

Answer 45

Prions are altered form of proteins and they can induce normal protein molecules to change their shape to the altered form.

Question 46

What is Kuru and hwo does it relate with prions and infectious protein folding?

Answer 46

Prions that mess up the shape of proteins cause Kuru a disease that was first found in an area where cannibalism is practiced( eating of the brain, which is very high in prions) and these prions cause proteins to have weird shapes(proteins that can make up the nervous system), this results in an attack on a persons nervous system causing them to laugh uncontrollably, have vast emotional mood swings and termors.