Chemistry of Life Flashcards

Unit 1

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

Polymer

A

A substance made of many similar units bonded together

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

Monomer

A

A single molecule that can be bonded to others to form a polymer

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

Nucleic Acid

A

Long-chain of nucleotides present in living cells ie.DNA and RNA

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

Nucleoside

A

base + sugar

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

Bases and H-bonding

A

Purines (2 rings) – pyrimidines (1 ring)
Adenine – Thymine/Uracil (2 H-bonds, weaker)
Guanine – Cytosine (3 H-bonds, stronger)
Hydrogen Bonding
(H with N, O or F)
-Slightly ionic (opposite charges)
-Slightly covalent ( H gets full shell, O/F/N does not)
-Strong because molecules are polar and H valence e- in closest shell so very strong attraction
-Very different electronegativities

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

nucleic bases descriptions

A

Purines (2-rings):
Adenine (no Oxygen, NH2 at top)
Guanine (1 Oxygen at top + NH2 on lower right)

Pyrimidines (1 ring):
Thymine (Oxygen at top and lower right, CH3 top right)
Uracil (Oxygen at top and lower right, smaller than T)
Cytosine (NH2 on top, Oxygen lower right only)

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

Van Der Waals Interactions

A

Dipole-dipole attraction
temp, perm (polar), H-bonding (perm + H-O/F/N)
-Weak between 2 atoms, accumulatively large within DNA structure
-Stronger when closer together
-Result of uneven e- distribution within molecules
-H-bonding within the base pair (A-T/U, G-C)

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

pH of bases

A

Phosphoric acid ion: H3PO4

  • Phosphate charge -1 (1 negative O2 atom because only 3H+ but 4O-)
  • DNA is a weak acid
  • Bases are weak base, acidic phosphates protect them
  • Attraction between nucleic acid and cation cloud
    • Strong electrostatic bond
    • Form strong ionic bond - donate e-
    • Stronger with larger difference in charges
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Organic Compound

A

Contains Carbon

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

Functional Groups

A

-INPUT FROM CHEM FLASHCARDS-

Phosphate H3PO4 -> H2PO4- (acidic)
Phosphodiester is phosphate with 2 ester bonds
amide is basic normally
amide is acid when in peptide bond

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

Amino acids

A

polarity:
H-bonding:
Hydrophilic/phobic

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

H-bonding
Donor
Acceptor

A

NH or OH functional group - H covalently bonded, high electronegativity
O or N functional groups - lone e- pair, dipole attraction to H nucleus (whose e- is more attracted to other covalent molecules as more electronegativity)
donate - loose H+
accepts - gains H+

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

Acid-base

A

Brønsted–Lowry
Acid - donates H+ NOTE: NH in Amide is not basic as donates H+
Base - accepts H+

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

stereochemistry

A

3D arrangement of molecules

double bonds cause fixed rotation

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

Chiral center

A

4 different sections off the center

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

Peptide bond

A

hydroxyl + amine forms amide and excess water
large chain of repeating structure
amide is acidic due to loosing H

17
Q

Fat Structure

A

Fatty acids linked to glycerol
Fatty acid - ester followed by long C chain (including double bonds at times)
Glycerol - 3-carbon unit connecting fatty acids
Try-glyceride - glycerol + 3 fatty acids

18
Q

Fat Properties

A
Hydrophobic
Even though ester groups present at one side
Long carbon chains unable to H-bond
Repels water and other H-bonding substances
Reduced interaction with H20
Increases entropy as things push apart
So clumps together separate to water
Polar head
Nonpolar tail
19
Q

Lipid Bilayer

A

Thin polar membrane of 2 layers of molecules
Prevents unintentional diffusion
Choline - hydrophilic polar head to create bilayer, hydrophobic fatty acid points inwards
Cholesterol - inserts itself within the layer to maintain rigidity under changing temperatures

20
Q

Glycogen

A

The storage form of glucose
Organised in 8-12 rings bonded together due to insulin
Stored in muscle and liver cells - closest to where it is needed, high blood supply present due to the activity of areas allowing for quick transport to other areas as needed
Lots of H-bonds so Hydrophilic so attracts water - need much more water to store glycogen than fat
Glycogen:water 1:3 or 1:4 ratio
Less energy efficient in storing energy than fat, as a result, more energy-efficient in releasing energy than fat
Benefits - quickly converted into energy, stores 6-8h at a time
Limitations - takes a while to restore stocks, takes a while to make glycogen

21
Q

Polysaccharide molecules

A

Polysaccharide – carbohydrate made of multiple sugar molecules bonded
Features:
Store energy from food
Cell structure

22
Q

Fats as energy

A

Mammals - fat slow-release energy store, difficult as fat hydrophobic
Migrating birds - more fatty acid transport protein to cope with this to allow easier conversion of fat to energy

23
Q

Enzyme Proteins

A

The catalyst for biochemical reaction, substrates -> products
specific to given reaction

24
Q

Defensive Proteins

A

Antibodies, found in the immune system

25
Q

Storage Proteins

A

Store metal ions and amino acids, found in plant seeds, eggs, milk

26
Q

Structural Proteins

A

Fibrous proteins keep physical structure ie. Keratin in hair, nails etc.

27
Q

Transport Proteins

A

Move molecules across the plasma membrane (passive, active)

Specific protein for each molecule transported

28
Q

Receptor Proteins

A

Receives chemical signals outside of the cell, cause cellular response ie. electrical
transmits instructions from outside cell into it

29
Q

Motor proteins

A

Motor - hydrolyse ATP to convert chemical energy into mechanical, move along cytoplasm of animal cells

30
Q

Contractile Proteins

A

Contractile - used in muscle contractions myofibrils (myosin and actin)

31
Q

Signalling Proteins

A

Signal endocrine system about hormone balance

regulates metabolism and cell function as a result

32
Q

Physical Structure

A

Primary – 2D wiggly line, determined by dna sequence
Secondary – 3D fold
Ɑ-helix – h-donation to below molecule, coiled structure
Β-strand – lateral h-donation, pleated snake structure
Tertiary – comprehensive 3D structure (over and under)
Hydrophobic Interactions – repel/attract
H-bonding – hold the structure in a given place
Ionic Bonding – opposite charged R groups come in close contact
Van der Wall or Covalent – stabilise
Quaternary – interaction between multiple chains (subunits)

33
Q

Similarity between structures

A

Proteins of similar sequence often fold in similar ways
Similar sequence means related strands of DNA
However, this does not necessarily mean they have a similar function
Similar structure:
Chicken Ovalbumin - egg white - main difference: V in code in place of R
Human Antithrombin - blood plasma - R in code in place of V
V = valine (C5H11NO2) - smaller, less H-bonding, molecules easier to separate
Donates and accepts
Hydrophobic
Charge:
R = arginine (C6H14N4O2) - larger, more H-bonding
Length width
Donates and accepts H+
Hydrophilic
Charge: positive