Chapter 2

Question 1

Covalent Bonds

Answer 1

Strong chemical bond where two atoms share electrons with the other

Question 2

Nonpolar

Answer 2

Equal sharing between atoms

Question 3

Polar

Answer 3

unequal sharing between atoms creating a partial positive partial negative region of the molecule

Question 4

Ionic Bonds

Answer 4

bond formed from the electrical attraction between two oppositely charged ions

Question 5

Ionic Bond example

Answer 5

Sodium wants to give up an electron and chloride wants to take it. As it does, they become attracted due to (+) and (-) charge once electron has been given up

Question 6

When is ionic bond strong

Answer 6

Strong when its dry

Question 7

Hydrogen Bond

Answer 7

weak electrostatic attraction between an electronegative atom and a hydrogen atom covalently linked to a second electronegative atom

Question 8

How does hydrogen bond work

Answer 8

Partial Negative atom that is attacked to Hydrogen that is linked to a electronegative atom

Question 9

Strength of Hydrogen Bond

Answer 9

Weak individual but enough of them working together can be quite strong

Question 10

Polar molecule

Answer 10

-Partial positive, partial negative
-Hydrophilic

Question 11

Non polar Molecules

Answer 11

Hydrophobic

Question 12

Amphipathic Molecule

Answer 12

-Nonpolar Region and a Polar Region

Question 13

How does Amphipathic molecule arrange

Answer 13

Arranges itself so all hydrophilic parts are together and by water and hydrophobic parts are together and away from water
-basic formation of the cell membrane to form

Question 14

Proteins

Answer 14

Chains of amino acids

Question 15

Amino Acid Structure

Answer 15

Amino group connected to Primary Carbon with R group connected to a carboxylic acid

Question 16

How do amino acids link together

Answer 16

Dehydration synthesis reaction
-OH comes off carboxylic group
-H off amino acid
-3 groups combine

Question 17

Primary Structure

Answer 17

Linear Structure of amino Acid

Question 18

Different types of amino acids

Answer 18

Polar, Nonpolar, charged

Question 19

Secondary Structure

Answer 19

Amino acid begin to interact with each other and start to fold

Question 20

Different folding structures

Answer 20

Alpha Helix- Coiling up
Beta-Sheet- Folding up itself (like a towel)

Question 21

How does the secondary structure interact

Answer 21

Ionic and hydrogen bonds and part of the structure can be alpha and can be beta

Question 22

Tertiary Structure

Answer 22

Different part of the same secondary structure begin to interact and from bonds

Question 23

How does the tertiary structure interact

Answer 23

Form ionic or hydrogen bonds and are a lot smaller and a lot more stable

Question 24

Breaking of bonds

Answer 24

Ionic and hydrogen bonds are collectively strong but individually weak so bond could be broken, and protein falls apart being denatured

Question 25

Quaternary Structure

Answer 25

two or more separate protein chains coming together to form a functional protein -only comes together by ionic or hydrogen bonds

Question 26

Factors affecting protein-ligan binding

Answer 26

Specificity Affinity Competition Saturation Modulation Environment

Question 27

Protein Specificity

Answer 27

A protein can be very specific for a particular ligand

Question 28

Affinity

Answer 28

-tightly the ligand and protein bind

Question 29

How does affinity work

Answer 29

-Share a lot of surface area and charge, together so it draws together -more bonds formed the more affinity

Question 30

Does specificity equal affinity

Answer 30

Specificity does not mean good affinifty

Question 31

Competition

Answer 31

-More than one ligand could bind to the protein -Forced to compete for the spot

Question 32

Saturation

Answer 32

-So much ligand that the protein is always going to have something bound to it -the protein cannot do anything faster than what it already is doing it at no matter how much ligand is around

Question 33

Modulation

Answer 33

-A way for a protein to turn on or off

Question 34

Allosteric Modulation

Answer 34

-Functional binding site allows a modulator molecule to bind causing the protein to flex -Ligand is capable of binding at a site for activation

Question 35

What happens when a modulator molecule is removed

Answer 35

-As soon as modulator molecule gets removed it should flex back causing deactivation

Question 36

Allosteric Inhibition

Answer 36

-Active protein -Ligand can bind -Regulatory molecule binds at another site non-covalently -Ligand in no longer able to bind -Protein is turned off

Question 37

Covalent Modulation

Answer 37

-Covalent bond was added at a site -Makes protein flex and change shape -Now a binding site is available for the ligand

Question 38

Most common way to covalently modulate

Answer 38

By adding a phosphate group, PO4 -Protein Kinase

Question 39

Covalent Inhibition

Answer 39

Bringing in protein kinase Adding a phosphate group Turning the protein off

Question 40

Environment

Answer 40

-Low temperatures does not interact -Molecules are not moving very quickly -warmer temperatures the molecules are moving -Interaction occur in the appropriate orientation for them to bind

Question 41

Why does optimal temperature have an affect

Answer 41

Optimal temperature is important to get the maximum interaction between the ligan and protein

Question 42

What happens after optimal temperature is reached

Answer 42

The protein will be under a lot of stress and can denature -it not longer has the specificity to interact with ligand

Question 43

pH

Answer 43

-low or high pH does not get a lot of interaction -optimum pH is important -different parts of the body have different optimal pHs