Lecture 4 Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

carbohydrates

A
  • molecules in which carbon is flanked by hydrogen and hydroxyl groups
    ( H — C —- OH)
  • contain a carbonyl group, several OH functional groups and many high energy C-H bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

generalized chemical formula of carbohydrates

A

(CH2O)n

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

why do cells use as an energy source?

A

glucose (monosaccharide)

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

2 forms of glucose

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

why do cells do with glucose during cellular respiration?

A
  • they oxidize glucose molecules to convert the stored energy to a form that can be readiliy used for cell work
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

why is glucose oxidized ?

A

so an organelle, the mitochondria, can make ATP

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

covalent bonds of glucose monomers

A

glycosidic linkagges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

2 types of glycosidic linkage

A

beta and alpha glucose chains

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

alpha glucose chains (def)

A
  • store chemic energy
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

type of alpha glucose chains

A
  • starch (plant energy storage)
  • glycogen (animal energy storage: liver & muscles)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

beta glucose chain (def)

A
  • form fibrious structures
  • straight chains held by many h bonds
  • highly packed, difficult to hydrolyze
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

type of beta glucose chains

A
  • cellulose (plants)
  • chitin (fungus & insects)
  • peptidoglycan (bacteria)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

different types of protein

A
  • enzymes
  • antibodies
  • motor proteins and contractile proteins
  • signalling molecules
  • structural molecules
  • transport molecules
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

enzymes

A
  • protein catalysts
  • speed up chemical reactions
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

antibodies

A
  • these are protein that protect the body from pathogens
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

motor proteins

A
  • can move molecules around inside of the cell
17
Q

contractile proteins

A

contract muscles in animals allowing them to move

18
Q

signalling molecules

A
  • cells can communicate by sending protein signals from one cell to the other
  • often called hormones
19
Q

structural molecules

A

gives cell a shape

20
Q

transport molecules

A

move molecules in and out of the cell

21
Q

proteins

A
  • chains of amino acids
22
Q

amino acids

A
  • have carboxyl and amino groups
  • they function as both acid and base
  • side chain varies from on amino acid to another
  • 20 different kinds
23
Q

bons between amino acid

A

peptide bonds

24
Q

chain of peptide bons

A

polypeptide chain

25
Q

r groups

A

differ in size, shape, reactivity and interactions with water

26
Q

nonpolar r groups

A
  • hydrophobic
  • do not readily dissolve in water
  • will sooner aggregate with other hydrophobic molecules
27
Q

polar r groups

A
  • hydrophilic
  • form h-bonds and readily dissolve in water
28
Q

primary structure of a protein

A

linear squence of amino acids/

29
Q

secondary structure

A
  • side groups within the amino acid chain interact causing the protein to fold into secondy structures
  • determined by the primary structure
  • h-bonds form between carbonyl groups, making them bend
30
Q

what can one change in amino acid do?

A
  • one change of amino acid can have drastic effects
31
Q

secondary structure patterns

A
  • alpha helix (coil)
  • beta pleated sheet (accordion)
32
Q

tertiary structure

A
  • result of interactions between r-groups in a polypeptide chain or between r-groups and peptide backbone
33
Q

interactions between r-groups

A
  • h-bonds
  • hydrophobic interactions
  • van der waals interactions
  • convalent disulfide bonds
  • ionic bons
34
Q

quaternary structure

A
  • several polypeptide chains can interact to form one protein
  • produce by the bonding of two or more polypeptid subunits
35
Q

protein structure

A
  • hierarchical
  • quaternary is based on tertiary, which is based on secondary
  • all 3 higher levels are based on the primary structure
36
Q

folding in proteins

A
  • proteins fold spontaneously when produced in a cell
  • fold into energetically stable form
37
Q

protein unfolding

A
  • stable form disrupted by high temperatures or low exposure to pH
  • proteins unfolds = denatures
38
Q

molecular chaperones

A

proteins that fold proteins