chapter two

Question 1

covalent bond

Answer 1

strong chemical bond where two atoms share electrons with the other

Question 2

nonpolar

Answer 2

equal sharing between atoms

Question 3

single covalent bond

Answer 3

hydrogen bond

Question 4

double covalent bond

Answer 4

oxygen

Question 5

polar

Answer 5

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

Question 6

ionic bonds

Answer 6

bond formed from the electoral attraction between two oppositely charged ions

Question 7

cations

Answer 7

sodium, potassium, calcium, hydrogen, magnesium

Question 8

anions

Answer 8

chloride, bicarbonate, phosphate, sulfate

Question 9

hydrogen bond

Answer 9

weak electrostatic traction between an electronegative atom and a hydrogen atom covalently linked to a second electronegative atom (hold molecules together DNA)

Question 10

amphipathic molecules

Answer 10

have charged and polar components to the molecule

Question 11

hydrophilic

Answer 11

has charge and dissolves well in water (polar or charged)

Question 12

hydrophobic

Answer 12

does not have a charge, does not dissolve well in water (non-polar)

Question 13

proteins

Answer 13

chains of amino acids, carry out actions of cell

Question 14

what are the four macromolecules?

Answer 14

nucleic acids (DNA, RNA), carbohydrates, proteins, fats / lipids

Question 15

peptides (proteins)

Answer 15

made up of long chains of amino acids linked together through the common portions of the structures with the functional groups hanging off the sides of the chain

Question 16

primary structure

Answer 16

linear sequence of the amino acids chain (any chain creates a different primary structure)

Question 17

secondary structure

Answer 17

protein folds, fold of the primary structure. creates the alpha helix (cork screw) and beta sheet (folds like a sheet)

Question 18

tertiary structure

Answer 18

when different secondary structures interact with one another (forms bonds with one another)

Question 19

quaternary structure

Answer 19

separate protein chains that come together to form a new larger protein

Question 20

factors affecting protein-ligand binding

Answer 20

specificity, affinity, competition, saturation, modulation, environment

Question 21

protein specificity

Answer 21

has very specific shape when it binds to its ligand (like a key in a lock)

Question 22

affinity

Answer 22

how much they like each other / will be drawn to one another, how strongly the molecules will bind together

Question 23

what does low affinity mean?

Answer 23

the ligand & protein come together strongly but will separate very readily

Question 24

what does high affinity mean?

Answer 24

will create bonds and hold it together as it moves around, the more bonds you form the higher the affinity

Question 25

competition

Answer 25

ligands compete to bind to the proteins, collisions based on concentrations

Question 26

saturation

Answer 26

is the protein bound to anything? once the ligand concentration becomes so great the protein is bound up 100% of the time

Question 27

what happens once you increase the ligand concentration?

Answer 27

there will be no more further impact

Question 28

modulation

Answer 28

control or regulate a protein

Question 29

what are the two types of modulation?

Answer 29

allosteric & covalent

Question 30

allosteric

Answer 30

can have multiple binding sites, non-covalently

Question 31

conformation

Answer 31

shape of a protein (how does it form), regulatory site and functional site change shape to fit ligand

Question 32

allosteric activation

Answer 32

inactive protein with a non compatible ligand, binds which causes protein to change shape, allosteric activator

Question 33

allosteric inhibition

Answer 33

a protein fits the ligand & binds which activates the protein, allosteric inhibitor binds non-covalently which causes protein to flex and ligand detaches

Question 34

covalent modulation

Answer 34

most common, binds to phosphate fro ATP, makes protein flex & change shape, the original primary binding site will fit a ligand, took a protein that didn’t work and turned it on

Question 35

what has to be involved in covalent modulation?

Answer 35

an enzyme (kinase)

Question 36

what does covalent modulation allow us to do?

Answer 36

turn proteins on or off depending on the need of the cell

Question 37

environment

Answer 37

temperature, pH

Question 38

what happens at low temperature?

Answer 38

at absolute zero molecules do not move

Question 39

what happens at high temperature?

Answer 39

molecules move faster which causes collisions and ability for them to bond, too warm can cause the protein to denature

Question 40

optimum temperature

Answer 40

maximum temperature, whatever temperature you might work best (37 degrees C for humans)

Question 41

what happens when we get too far away from the optimum temperature?

Answer 41

denatures the protein pH