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Organic Chemistry Flashcards

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1
Q

What type of bond in Nucleic acids in nucleotides

A

Phosphodiester

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2
Q
A

Alcohol

Hydroxyl

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3
Q

Cell Wall

A
  • gives, cell shape / strength / support;
  • prevents bursting (when water enters cell by osmosis);
  • fully permeable;
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4
Q

The bond that joins the two molecules to form a disaccharide

A

Glycosidic

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5
Q
A

Carboxyl

Esters

Esters are a combination of a carboxylic acid and an alcohol where the O-H from the carboxylic acid and the H from the alcohol combine to form water

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6
Q
A

Termination of Free Radical

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7
Q
A

Amino

Amines

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8
Q
A

Chloroplast

Cell Wall

Vacuole

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9
Q

DNA

A
  • deoxyribose (sugar)
  • phosphate (group);
  • nitrogenous / purine or pyrimidine) base
    • Adenine
    • Guanine
    • Cytosine
    • Thymine
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10
Q

Hex-

A

6C

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11
Q

What type of bonds in Monosaccharides units in sugar

A

Glycosidic

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12
Q

Active Site

A

The area on enzyme to which a substrate binds

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13
Q
A

A - Glycoprotein - Interegal Protein: carrier molecule

B - Phospholipid Bilayer - waterproofing

C - Carbohydrate - receptor

D - Cholesterol: Provide structure, regulate fluidity

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14
Q

Oct-

A

8C

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15
Q
A

Initiation of Free Radical

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16
Q

plasma (cell surface) membrane

A
  • controls exchange between cell and environment / selectively permeable; R water
  • receptors for, cell recognition / attachment;
  • fluid to allow, endocytosis / exocytosis;
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17
Q

Nucleic Acid

A

Sugar/base/phosphate

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18
Q

Metaphase

A

The chromosomes align on the equator of the spindle

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19
Q

CoFactor

A

The general name given to a non-protein helper which helps an enzyme to function

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20
Q

Induced fit hypothesis

A

The model of enzyme-substrate binding whereby an enzyme adjusts to fit the substrate

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21
Q

Golgi Apparatus

A

processes, molecules / proteins; AW

use in secretion

lysosome formation

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22
Q

Competitive Inhibitor

A
  • substrate and inhibitor are a similar shape
  • able to, bind / fit into / block, active site;
  • (shape) complementary to active site
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23
Q
A

Tertiary Amine

3H have been replaced by R Groups

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24
Q

Mitochondria

A
  • formation ATP / suitable energy ref.;
  • aerobic respiration;
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25
Q
A

A - Golgi apparatus/body

B - Centriole

C - Nucleolus

D - Nuclear Membrane or Nucleus

E - Mitochondrion

F - Rough Endoplasmic Reticulum

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26
Q

Cholesterol

A

lipids / cholesterol, hydrophobic / non-polar

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27
Q
A

They share an O and lose 2H and O

Its a condensation reaction resulting in 3 H2O

Ester bond

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28
Q
A

U - Amino

V - Carboxylic Acid

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29
Q

Tissue

A

collection / group, of cells (of one or more types); [1]

(cells), working together OR with, common / same, function; [1]

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30
Q

Vacuole

A
  • reservoir of, salts / sugars / waste / pigment / other e.g.;
  • ref. to, turgor / support / controlling Ψ (Water Potential)
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31
Q
A

Halo

Halogen-hydrocarbons

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32
Q
A

Geometric Isomer

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33
Q

Nucleus / DNA

A
  • controls, activities of cell / transcription / named activity / cell division;
  • contains genetic information that can be transmitted to next generation;
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34
Q
A

Structural Isomer

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35
Q

Formation of Primary Structure of Protein

A

Amino acid monomers join to form a dipeptide [1]

Process involves removal of water and is a condensation reaction [1]

A carboxyl group from amino acid (OH) is removed together with an H atom from another acid [1]

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36
Q

But -

A

4C

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37
Q

Protein Production in Rough ER

A
  • Proteins are pinched off vesicles in the Rough Endoplasmic Reticulum/RER
  • Proteins are transported in vesicles to the Golgi Apparatus
  • Proteins are modified in the Golgi Apparatus/Have carbohydrates added to the proteins
  • Modified proteins are placed into vesicles
  • Modified proteins are released from the plasma membrane/Exocytosis
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38
Q
A

Primary Amine

Replace 1 H with an R group

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39
Q

RNA

A
  • ribose (sugar);
  • uracil instead thymine
  • single stranded
  • 3 forms (RNA, mRNA, tRNA)
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40
Q
A

Carboxyl

Carboxylic Acids

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41
Q

What type of bond in Fatty acids to glycerol in triacylglycerols

A

Ester

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42
Q

Prosthetic Group

A

The name given to an ion which is permanently attached to an enzyme so that it may carry out its function

43
Q

• cytoplasm

A

• site of chemical reaction(s)

44
Q
A

J - Channel protein

K - Receptor, Recognition site, helps to adhere one to the other

M - Cholresterol - Adds structure

L - Phospholipid bilayer - waterproof barrier

45
Q
A

Double Bond

Various Unsaturated

46
Q

Nucleolus

A

Produces, ribosomes / rRNA

47
Q
A

A - Smooth Endoplasmic Reticulum

B - Nuclear envelope

C - Mitochondia

D - Nucleolus

E - Lysosome

F - Rough Endoplasmic Reticulum

48
Q

The Krebs Cycle

A
  • Acetyl co-enzyme A combines with oxaloacetate to from citrate
  • Citrate is decarboxylated and dehyrogenated to yield carbon dioxide (waste gas) and hydrogen (combines with carriers NAD and FAD)
  • 5 carbon molecules is created which is decarboxylated and dehydrogenated c
  • Reduced FAD and 4 carbon molecule is created
  • This is converted to another 4 carbon molecule and ATP is released
  • This 4 carbon molecule is dehydrogenated
  • Another 4 carbon molecule is created and redFAD
  • Dehyrogenated occurs, reduced NAD is created
  • Oxaloacetate is regenerated
49
Q
A

Alkoxy

Ethers

50
Q
A

Thiol

Thiols

51
Q

The Link Reaction

A
  • Pyruvate has carbon dioxide removed/decarboxylated
  • It also has hydrogen removed- dehydrogenated
  • It combines with Co-Enzyme A to give acetyl co-enzyme A
52
Q
A
53
Q

Proteins

A

Amino Acids

54
Q
A

A - beta - Glucose

B - 1,4 glycosidic beta link

Reaction

  • condensation/removal of water

Function of cellulose

  • Cell wall of plants
55
Q

Rough ER / ribosomes

A

• protein synthesis

56
Q

Cellulose

A

ß-glucose

57
Q

Chloroplast

A
  • photosynthesis
  • chlorophyll / pigment, absorbs light
58
Q

Temperature and Enzymes

A

High

  • (enzyme) increases in kinetic energy or ‘too much kinetic energy’
  • enzyme vibrates too much;
  • breaks bonds;
  • changes, tertiary/3-D, structure/shape, of enzyme;
  • active site changes, shape
  • substrate will not fit/no enzyme-substrate complex formed;
  • enzyme denatured;
  • will, decrease rate/stop reaction;

Low

  • not enough kinetic energy
  • inactive
59
Q

Hept-

A

7C

60
Q
A

Propogation of Free Radicals

61
Q

Fats

A

Fatty acids, gycerol

62
Q

Prop -

A

3 C

63
Q

Glycolysis (Formation of Pyruvate)

A
  • Glucose is phosphorylated/has a phosphate added
  • Using a molecules of ATP
  • Creates hexose phosphate
  • Second ATP molecule is attached to create hexose bisphosphate
  • Hexose bisphosphate breaks down to produce two molecules of triose phosphate
  • Triose phosphates are phosphorylated
  • Using free Pi ions
  • Hydrogen is removed from each triose phosphate/triose phosphate is dehydrogenated
  • The H+ ions are transferred to carrier molecules NAD and are used later
  • This yields 2 molecules of pyruvate
64
Q

Anaphase

A

The chromatids separate and move to the poles

65
Q

What type of bond in Amino acids in proteins

A

Peptide Bond

66
Q
A

Trans

67
Q

Formation of the Tertiary Structure of a Protein

A

Proteins fold to form coiled coils [1]

The tertiary structure is the way the regions of secondary structure fold to form the 3-D shape i.e. a-Helices and b-Pleated sheets [1]

4 possible create the tertiary structure; Disulphide bridges, Ionic Bonds, Hydrogen bonds, Hydrophobic Interactions [1]

68
Q

Smooth ER

A

Makes / transports, lipids / steroids / hormones; A named plant e.g.

69
Q

Non-

A

9C

70
Q

Glycogen

A

a-glucose

71
Q

Dec-

A

10C

72
Q

Lysosome

A
  • hydrolytic / digestive, enzymes
  • breakdown, organelles / cell / ingested material
73
Q
A

Amide

Amides

74
Q
A

Carbonyl

Aldehydes

75
Q

Boiling Points of Alkanes

A

0 at 4C

Goes up by approx 30-36 degrees per Carbon

The boiling point increases with increase in molecular formula of carbon atoms/chain length

Because more intermolecular forces/electrons/surface area/ Weak intermolecular forces (van der waals)

76
Q

Formation of Quaternary Structure of a Protein

A

The quaternary structure is the association of more than one polypeptide chain [1] •

Haemoglobin is made of 4 polypeptide chains stabilised by inter- & intramolecular bonds [1]

Network of non-covalent interactions [1]

77
Q

Eth -

A

2 Carbons

78
Q

Meth -

A

1 Carbon

79
Q

Non-Competitive Inhibitor

A
  • reduces reaction rate;
  • fits into, allosteric site / site other than active site;
  • alters, shape / charge, of active site;
  • so substrate cannot, fit to active site / bind to active site / form ESC;
  • increasing substrate concentration has no effect (on the rate);
80
Q

DNA Replication

A
  • The double helix untwists
  • Is then unzipped by the breaking of the H bonds via DNA helicase
  • Free nucleotides are attracted to their complementary bases
  • C to G (3 H Bonds) and A to T (2 H bonds)
  • Hydrogen bonds reform
  • Sugar phosphate back bone forms using covalent/phosphodiester bonds using DNA Polymerase
81
Q

Molecular Structure of Glycogen

A
  • polymer/polysaccharide/described;
  • (made of) α-glucose; joined by 1,4 links;
  • (chain is) branched;
  • 1,6 glycosidic links where branches attach; compact
82
Q

Oxidative Phosphorylation and Chemiosis

(The Electron Transport Chain)

A
  • Hydrogens are split from FAD (at complex II) and NAD (at complex I)
  • Hydrogen is broken into H+ and an electron.
  • The electron is transferred along the electron transport chain
  • H+ ions are pumped across Complexes I, III and IV into the intermembranal space
  • H+ ions diffuse through ATP synthase from the intermembranal space into the mitochondrial matrix
  • ATP is created
83
Q

Telophase

A

The nuclear membrane reforms and cytokinesis follows.

84
Q
A

Carbonyl

Ketones

85
Q

Formation of Secondary Structure of a Protein

A

a -Helices – Forms H bond between the C=O group of one amino acid and the N-H group of an another amino acid [1]

ß-Sheet – From interactions between adjacent chains, held in close association by H bonds between C=O and N-H groups on the different strands [1]

86
Q

Essential Fatty Acids (2)

A

Fatty acids that cannot be synthesised by the body [1]

They must be supplied/taken in by the diet [1]

Omega-3 anti-inflammatory

Omega-6 pro-inflammatory

87
Q

Pent-

A

5C

88
Q
A

Secondary Amine

Replace 2 H with R group

89
Q

Rough ER

A

• transport of proteins

90
Q

Prophase

A

The chromosomes become stainable and the spindle starts to form

91
Q
A

Cis

92
Q
A

A. phospholipid layer/bilayer

B Cholesterol

C Glycolipid

D Carbohydrate

93
Q

Outline how haemoglobin acts as a pH buffer in the presence of carbon dioxide.

A
  • Carbon dioxide combines with water to form carbonic acid
    • H2O + CO2 –> H2CO3
  • Carbonic acid splits into hydrogen ions (H+ ) and hydrogen carbonate ions (HCO3- )
    • H+ and HCO3 –
  • The reaction is catalysed by carbonic anhydrase
  • The hydrogen ions produced combine with haemoglobin to from haemoglobinic acid
  • This causes it to release its oxygen which diffuses into respiratory tissue
  • Hb is acting as a buffer, helping to keep the pH of blood around 7.4
94
Q
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