Lecture 2- Chemical Bonds and Macromolecules Flashcards

(52 cards)

1
Q

Why is water the solvent of life?

A
  • polar (has partial charges- unequal distribution of e- across a bond)
  • oxygen has a high affinity for e- (high electronegativity) so the e- sit closer to O than to H
  • anything that can interact with a charge can interact with water
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

explain the relationship between water and a nonpolar substance

A

they cannot form favorable interactions; they nonpolar molecule will aggregate (clump together away from the water) like oil

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

organic molecules contain __ and ___

A

carbon and hydrogen

  • C is the backbone of organic molecules
  • C is weakly electronegative
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Why is life carbon based? List 3 reasons

A
  1. C can bond to 4 other atoms (lots of diversity from one single backbone)
  2. C can bond to form C-C chains (long!)
  3. C can form double bonds and triple bonds

all of this results in a lot of molecular diversity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Define monomer

A

“single unit”

single building block of a macromolecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

define polymer

A

“multiple units”
a chain of monomers composed of similar yet non-identical subunits (similar in that they’re all amino acids, but there are 20 amino acids)
eg. a molecule of DNA is a polymer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

why are polymers more biologically important that monomers?

A

they allow for variation to promote biological diversity

  • eg. proteins have 20 amino acids- endless diversity
  • eg. DNA; 4 nucleotides in combination
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

polymers must be built up/ broken down by the ___

A

cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

synthesis of polymers is done by ____

A

condensation/ dehydration reactions

eg. DNA replication

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

explain a condensation/ dehydration rxn

A
  • add monomers to a growing chain; formation of covalent bonds
  • water is a product
  • requires energy (building up a polymer!)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

the breakdown is polymers is done by a ___ reaction

A

hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

explain a hydrolysis rxn

A
  • cleavage of covalent bonds between monomers in a polymer (the bonds holding the polymer together)
  • water is a reactant
  • releases energy
  • breakdown of a polymer!
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

function and structure of carbohydrates/ polysaccharides/sugars

A
  • energy storage
  • cell structure (cellulose in plant’s cell walls)
  • cell-cell recognition
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

monomers of carbohydrates

A

CH2O (monosaccharides)

  • monomers have a C chain of 3-7C long
  • can be linear or ring shaped
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

describe an example of a carbohydrate

A

glucose (C6H12O6)

  • main energy source in cell
  • reactive H and OH groups allows extensibility (react w/ reach other –> long chains)
  • ring shape dominates in the cell
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Disaccharides are formed by

A

a covalent bond between monosaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

example of a disaccharide

A

disaccharide of glucose(6C) = fructose (6C)

- structural isomers (same formula, different shape)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

bond type in carbohydrates

A

glyosidic bond
- Carbohydrates are made up of monosaccharides linked together into polysaccharide chains by a type of covalent bond known as a glycosidic bond. These glycosidic bonds are formed in a dehydration synthesis reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Glycogen is a _____ polysaccharide (a polymer of ___ that’s highly branched)
- Function of glycogen?

A

nutritional
glucose
Function: energy storage in animals

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

polysaccharides are ____ of _____

A

polymers of monosaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Difference b/w structures of starch vs cellulose

A

starch: OH all on same side
Cellulose: OH on alternating sides

22
Q

name 4 polymers of glucose and their functions

A
  1. starch: fxn= energy storage in plants
  2. glycogen: fxn= energy storage in animals
  3. Cellulose: fxn= plant cell wall
  4. Chitin: fxn= insect exoskeleton and fungal cell wall
23
Q

True/ False

Lipids/ fats are true polymers

A

False

macromolecule? arguable

24
Q

How to you classify a lipid?

Fxn of lipids?

A

hydrophobic

  • non-polar and aggregate away from water
  • made up of mostly H and C

fxn= energy storage and insulation

25
Fatty acids are a single chain (usually ___ C long) with a ____ end - they can attach ("____") to a glycerol backbone
16-18 COOH esterify
26
Fatty acids can be saturated or unsaturated. Explain the difference
saturated: all single C-C bonds Unsaturated: double carbon bond (causes kink in the fatty acid tail)
27
phospholipids are the structural component of ____ | - they are ___(have both hydrophilic and hydrophobic domains)
membranes | -amphipathic
28
``` Steroids are a class of lipids based on _____ - characterized by the backbone of 4 ____ ___ ```
cholesterol | 4 fused rings
29
2 major fxns of steroids
1. hormones: eg estrogen, testosterone, progesterone | 2. in animals, cholesterol sits in plasma membrane to maintain fluidity and increase membrane stiffness
30
Proteins are polymers of ___ ____ | - what's the directionality?
amino acids | - N to C (amino- NH3+ to carboxy- COO-)
31
why are amino acids extendible? | ie why is it possible to make the polymer (proteins)
amino acids carry both a negative (COO-) and positive (NH3+) charge. Therefore the amino and carboxy (acid) groups are reactive/ extendible
32
4 possible R (variable) groups of proteins:
1. non-polar (R=CH) 2. polar uncharged (R= -OH or -SH) 3. Polar uncharged acidic (R= COO-) *neg charge 4. Polar charged basic (R= NH3+) *pos charge
33
what kind of bond do proteins have? | ie. a.a. are linked covalently by ___ bonds
peptide
34
Are R groups involved in polymerization? | What happens to the directionality as the amino acids are polymerized?
- no, R groups are not involved in polymerization | - N to C directionality is maintained in the polymer
35
the primary structure of a protein is the polymer of a.a. (N to C) What does the primary structure dictate?
It dictates folding (what a.a. in what order?) | *a.a. sequence determines folding and folding dictates function
36
Describe the secondary structure of proteins
interaction b/w the backbone of the peptide chain (r-groups drive the folding, but do NOT stabilize it) - the secondary structure= local folding of a.a. chain into either alpha helix or beta sheet * stabilized w/ H-bonds b/w a.a. backbones
37
characteristics of alpha helix vs beta sheet
beta sheet: fully stretched out | alpha helix: coiled region of protein
38
the tertiary structure is the ___ pattern of protein folding
3D
39
what is the driving force of folding for the tertiary structure?
hydrophobic interactions of non-polar R groups drive a.a. away from water into middle of the protein
40
The forces that maintain the tertiary structure are interactions between R-groups. List the types of stabilizing interactions from strongest to weakest.
1. (strongest): Covalent bonds: disulfide bridges b/w 2 cysteine 2. ionic bonds (b/w oppositely charged a.a.) 3. Hydrophobic interactions: b/w non-polar a.a. 4. (weakest): H-bonds (b/w polar, uncharged a.a. (dip-dip)
41
Describe the quaternary structure. | What forces holds it together?
- some proteins form multisubunit complexes that create a functional protein - quaternary structure held together by the same forces as the tertiary structure (R-group interactions)
42
____ are proteins that assist in the folding of other proteins
chaperones
43
list some examples of human diseases of protein folding
mad cow disease Alzheimer's Parkinson's sickle cell anemia (can be caused by a few things)
44
describe the steps of a bacterial chaperonin
1. unfolded protein enters folding chamber 2. chamber provides a favorable environment for folding 3. chamber spits out a correctly folded protein * can refold protein that's been unfolded by heat for ex
45
Function of nucleic acids
- store/ transmit heredity info - Rna transmits info within cell - DNA transmits info b/w cell generations
46
Describe the 2 types of nucleic acids
1. DNA: - polymer of deoxynucleotides (DNA ntds are deoxygenated at carbon 2 of ribose sugar) - contains all info essential for life 2. RNA: - polymer of ribonucleotides - many functions for RNA: - info= mRNA - translation= tRNA and rRNA - regulation= siRNA, miRNA - splicing= snRNA
47
Basic structure of a ntd (3 components)
1. 5- carbon sugar = ribose 2. nitrogenous base 3. phosphate
48
What does each carbon do in ntds?
``` C1: attaches to the base C2: in DNA, there's no OH, in RNA there is an OH C3: 3' OH (essential for polymerization) C4: boring carbon C5: attaches to PO4 ```
49
monomers are joined into sugar-phosphate backbone by ______ linkages. - the backbone is ____ charged with the bases pointing off of the backbone
phosphodiester linkages - negatively
50
A and T have ___ H-bonds | G and C have ___ H-bonds
``` A/T= 2 bonds C/G= 3 bonds ```
51
why does a purine (A and G) always pair with a pyrimidine (C and T- or C and U)?
to maintain the diameter of the helix
52
why is RNA single stranded?
2' OH makes helix more open and reactive therefore the free base pairs with itself, other RNA, or DNA