Ch. 3 The Chemical Basis of Life Flashcards

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

Functional groups

A
  • groups of atoms with special chemical features that are functionally important
  • each type of functional group exhibits the same properties in all molecules in which it occurs
  • most organic molecules and macromolecules contain functional groups
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
1
Q

Condensation/dehydration reaction

A
  • links monomers to form polymers
  • generates one water molecule for each monomer added
  • can repeat for thousands of monomers
  • catalyzed by enzymes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Carbohydrates

A
  • Cn(H2O)n
  • most of the carbon atoms in a carbohydrate are linked to a hydrogen atom and a hydroxyl (OH) group
  • composed of carbon, hydrogen, and oxygen atoms
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Monosaccharides

A
  • monomers of carbohydrates
  • pentoses (5 Cs)
    • ribose and deoxyribose
  • hexoses (6 Cs)
    • glucose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Disaccharides

A
  • composed of two monosaccharides
  • joined by dehydration/condensation
    broken by hydrolysis
  • joined by glycosidic bond
  • ex: sucrose, maltose, lactose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

hydrolysis

A
  • polymers broken down into monomers
  • a molecule of water is added back each time a monomer is released
  • can repeat to break down long polymers
  • catalyzed by enzymes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Glycosidic bond

A

covenant bond that joins monosaccharides to form carbohydrates

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

polysaccharides

A
  • maney monosaccharides linked together to form long polymers
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

two types of Energy storage polysaccharides

A
  • starch (plants)
  • glycogen (animals)
  • structure is more branched, so it can be broken down more easily, making it a good energy source but doesn’t have good structural integrity
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Structure polysaccharides

A
  • Cellulose
  • chitin
  • glycosaminoglycans
  • since, its more condensed and has H-bonding between the layers, it is better for structure but isn’t broken down as easily for energy
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Fats/triglycerides

A
  • Formed by bonding glycerol to 3 fatty acids
  • joined by dehydration; broken by hydrolysis
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Saturated fats

A
  • all carbon linked by single bonds
  • tend to be solid at room temperature
  • fully saturated in C-H bonds
  • animal fats usually saturated
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Unsaturated fats

A
  • contain one or more double bond
  • tend to be liquid at room temp.
  • cis forms naturally
  • trans formed artificially & is linked to disease
  • plant fats usually unsaturated
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Phospholipids

A
  • formed from glycerol, two fatty acids, and a phosphate groups
  • amphipathic molecules (polar phosphate head w/ non polar fatty acid tail)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

phospholipid bilayer

A
  • can be more or less fluid depending on the types of phospholipids that make it up
  • each side is called a leaflet of phospholipids
  • the individual phospholipids are independent of each other (not bonded)
  • trapped in place by polarity
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Proteins

A
  • peptide/polypeptide with a specific function
  • composed of C, H, O, N and small amounts of other elements like S
  • made of amino acids
16
Q

lipids (makeup and examples)

A
  • composed of predominantly hydrogen and carbon atoms
  • non polar
  • includes fats, phospholipids, steroids, and waxes
  • on average, make up about 40% of organic matter in the human body
17
Q

amino acids

A
  • monomers of proteins/polypeptides
  • 20 types of amino acids
  • amino group - positively charged
  • R group - side chain that determines structure and function
  • carboxyl group - negatively charged
18
Q

Polypeptide formation

A
  • amino acids join to form peptide bonds via dehydration reaction
  • proteins may be formed from one or several polypeptides
  • a polypeptide isn’t necessarily a protein
19
Q

primary protein structure

A
  • amino acid sequence
  • encoded directly by genes
  • first amino acid will always have its amino group exposed (amino terminus)
  • last amino acid will always have its carbonyl group exposed (carbonyl terminus)
20
Q

Secondary protein structure

A
  • chemical and physical interactions cause protein folding
  • alpha helices and beta pleated sheets are key determinants of a protein’s characteristics
  • “random coiled regions” - not helix of pleated sheet
  • shape is specific and important to function
21
Q

Tertiary protein structure

A
  • folding gives proteins complex 3D shapes
  • final level for a single polypeptide chain
22
Q

Quaternary structure

A
  • made of two or more polypeptides coming together to change the functionality
  • ## made of individual polypeptides called protein subunits
23
Q

5 factors promoting protein folding and stability

A
  1. H-bonding
  2. ionic bonds and other polar interactions
  3. hydrophobic effects
  4. Van der Waals forces
  5. Disulfide bridges
24
Q

Protein-protein interactions

A
  • polypeptides must fit by both shape and charge
  • four factors to bind:
    1. H-bonding
    2. ionic bonds and other polar interactions
    3. hydrophobic effects
    4. Van der Waals forces
25
Q

glucose isomers

A

ex: glucose and galactose
- alpha glucose - hydroxyl group below ring
- beta glucose - hydroxyl group above ring
-

26
Q

what affects how proteins interact

A
  • hydrogen bonds
  • ionic bonds and other interactions
  • hydrophobic effects
  • Van der Waal forces
  • protein conformation (must fit)
  • likely no covalent bonds
27
Q

modules/domains of proteins

A
  • distinct structures of proteins that have specific functions
  • proteins that share a particular domain also share the associated function
28
Q

two classes of nucleic acis

A
  • deoxyribonucleic acid (DNA)
  • ribonucleic acid (RNA)
29
Q

DNA vs. RNA

A
  • DNA stores genetic information encoded in the sequence of nucleotide monomers
  • RNA decodes DNA into instructions for linking together a specific sequence of amino acids to form a polypeptide chain
  • both made from nucleic acids
  • DNA has thymine, RNA has uracil
  • DNA has one form and RNA has several
  • RNA has some enzymatic functions
30
Q

3 parts of a nucleic acid

A
  • phosphate group
  • five-carbon sugar (ribose or deoxyribose)
  • nitrogenous base
31
Q

types of nitrogenous bases

A

purines
- Adenine and Guanine
- have two rings
pyrimidines
- cytosine and thymine
- have one ring
Cytosine-Guanine is stronger because it has 3 H-bonds instead of 2

32
Q

Structure of DNA

A
  • two strands in a double helix
  • 3’ of one carbon connects to the 5’ of the next
    -3’ exposed on one side, 5’ on the other
33
Q
A