Molecules of Life Flashcards

1
Q

Bonds

A
Covalent
Other types
- Ionic
- Hydrogen
- Van der Waals interactions
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Covalent Bonds

A

A covalent bond is the sharing of a pair of valence electrons by two atoms

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

Van der Waals Interactions

A

Dipole-dipole
Dipole-induced-dipole
Dispersion

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

Water

A

The solvent of life
Cohesive (the molecules stick to one another due to hydrogen bonds), allowing to have surface tension
Moderates temperature changes (high specific heat capacity; evaporative cooling)
Ice is less dense than its liquid form (due to having 4 H-bonds, which require a certain distance between the molecules, instead of 2); however, cold liquid water is denser than when it is warm
Hydrophilic
2 molecules dissociate to form Hydronium and Hydroxide (2H_2O ⇌ H_3O^+ + OH^−)

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

Carbon

A

Often forms bonds to itself
Forms four covalent bonds
Can form double bonds
Is versatile

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

Isomers

A
Have the same number and type of atoms
Structural isomers (same formula, different structure)
Geometric isomers (different arrangement of atoms around a double bond)
Enantiomers (mirror images of each other)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Polymers

A

Grouping of multiple monomers
Can be created through a dehydration reaction
Can be broken through hydrolysis

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

Macromolecules of Life

A

Carbohydrates (sugars)
Proteins (amino acids)
Lipids (fatty acids)
Nucleic acids (nucleotides)

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

Carbohydrates

A
Role
- Fuel
- Structure
Monosaccharides, disaccharides, polysaccharides
C_n(H_2O)n → C_nH_2nO_n
Different types
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Glucose

A

C_6H_(12)O_6
A hexose
Most of it in our body is in ring formation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Glycosidic Bonds / Glycosidic Link

A

Formed from a dehydration reaction (an H_2O escapes)

An oxygen atom forms a bond between the two molecules

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

Maltose

A

α-glucose + α-glucose forming a 1-4 glycosidic link

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Sucrose

A

α-Glucose + β-Fructose forming a 1-2 glycosidic link

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Lactose

A

β-galactose and α-glucose forming a 1-4 glycosidic link

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Glycogen

A

Animal storage of sugar
Linked and branched glucose
α1-4 and α1-6 glycosidic links

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Starch

A

Plant storage of glucose

Amylopectin and Amylose

17
Q

Amylopectin

A

Branched glucose
Makes up 70% of starch
α1-4 and α1-6 glycosidic links

18
Q

Amylose

A

Unbranched glucose
Denser than Amylopectin
α1-4 glycosidic links

19
Q

Cellulose

A

Structural

Straight (not helical) due to β1-4 linkages between glucose

20
Q

Nucleic Acids

A

Transmit and store genetic information
DNA (complementary bases in double helix) and RNA
Monomers are called “nucleotides”

21
Q

Nucleotide

A

Made up of a phosphate group, a sugar (pentose) and a nitrogenous base, the latter two forming the nucleoside
The sugars are either Deoxyribose (in DNA) or Ribose (in RNA)
The nitrogenous bases are either pyrimidines or purines

22
Q

Pyrimidines

A

Cytosine (C)
Thymine (T, in DNA)
Uracil (U, in RNA)

23
Q

Purines

A

Adenine (A)

Guanine (G)

24
Q

Phosphodiester Bond

A

Bond between two nucleotides, with the phosphate group involved

25
Proteins
Effectors of most cell functions Widely diverse Can be delicious
26
Amino Acid
Contains a central carbon atom attached to a hydrogen atom, to a carbonyl group, to an amino group and to a variable side chain Amphipathic The side chain can be non-polar (hydrophobic), such as glycine (Gly, G) and proline (Pro, P), or it can be electrically charge (either positively - basic - or negatively - acidic - charged) or polar (the latter two being hydrophilic)
27
Zwitterions
Dipolar ions | Change depending on pH
28
Peptide Bond
Caused by a condensation reaction in which an H_2O escapes to link the C and N atoms of two amino acids
29
Polypeptide Chain
Protein | Many amino acids linked with peptide bonds
30
Protein Functions
Catalysts (in our body, enzymes) Amino acid storage Coordination of an organism’s activities (insulin, secreted by the pancreas, causes other tissues to take up glucose, thus regulating blood sugar concentration) Movement Protection against disease (activates antibodies) Response of cell to chemical stimuli Support
31
Denaturation
Breaking side chain interactions in a protein, creating a denatured protein Caused by pH, temperature, solvents…
32
Renaturation
Reforming side chain interactions in a protein, usually by cells, creating a normal protein Protein folding is a significant area of research: Fibrosis, Alzheimer’s, Parkinson’s, Creutzfeldt-Jakob disease…
33
Lipids
No common structure (grouped by property instead) Hydrophobic Varying functions depending on the type of lipid Types of lipids: fatty acids, phospholipids, steroids
34
Triglycerides / Triaglycerols
``` Fatty acids Always hydrophobic Serve as storage Include ester bonds Form by releasing three H_2O molecules ```
35
Phospholipids
Glycerol with two fatty acids Varying polar head group, but always hydrophilic Amphipathic Create cell membranes Unsaturated fatty acids increase fluidity Can form bilayers
36
Steroids
``` Lipids Derived from four fused rings Largely hydrophobic (amphipathic) Can play many roles Cholesterol disrupts cell membranes Hormones, vitamin D ```
46
Hydrogen Bonds
H-bonds form when the partial positive charge of hydrogen atoms are attracted to the partial negative charge of oxygen atoms