Molecular building blocks Flashcards

1
Q

What are basic building blocks atoms?

A

Carbon
Hydrogen
Oxygen
Nitrogen
Sulphur
Phosphate

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2
Q

What are macromolecules? E.g.

A

Simple molecules (sugars, lipids, aa)
Form larger
Osmotic, structural, optical, enzymatic
E.g. Hb, DNA, glycogen, collagen

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3
Q

What is a monosaccharide?

A

One hydroxyl
Aldose- aldehyde
Ketose- ketone
Ring structure

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4
Q

What bond is present in carbohydrates?

A

Glycosidic bond
Hydroxyl react with OH/NH

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5
Q

What bond is present in nucleotide DNA?

A

N-Glycosidic

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6
Q

Define disaccharide?

A

Two monosaccharides joined by o-glycosidic bond

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7
Q

Define oligosaccharide?

A

3-12 monosaccharides

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8
Q

Define polysaccharide?

A

1000’s MS joined by glycosidic bond
e.g. glycogen

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9
Q

What are building blocks of DNA? Made?

A

Nucleotides
Nitrogenous base, sugar, phosphate

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10
Q

What are bonds involved in nucleotides?

A

Bases- Hydrogen bonds
Phosphate and sugar- Phosphodiester
- source energy

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11
Q

Structure of triglyceride?

A

3 FA bound to glycerol

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12
Q

What makes up lipid?

A

Straight carbon chain with methyl and carboxyl group

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13
Q

Lipids hydrophilic/phobic?

A

Hydrophobic

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14
Q

What is it called when double bond present?

A

Unsaturated
Cis- spaced 3C

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15
Q

What bonds in protein?

A

Aa- linked by peptide bonds
Protein- large polypeptide 10-1000’s aa
Peptide- bit broken off

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16
Q

What decides function of protein?

A

Structure

17
Q

What determines folding of proteins?

A

Charged interactions, flexibility, aa seq, physical dimensions

18
Q

What are the different structures of protein?

A

Primary- linear sequence of amino acids
Secondary- alpha helix or beta pleated
sheets
- formed due H+ bonds between
aa
Tertiary- overall 3D conformation
- change with temp/pH
Quaternary- 3D structure of protein-
multiple subunits
- association subunits

19
Q

What forces are involved in proteins?

A

VdW’s- weak attractive/repulsive force
- fluctuating electrical charge
Hydrogen bonds- interaction polar groups
Hydrophobic- uncharged, nonpolar repelled
Ionic- fully/partially charged groups
Disulphide- strong covalent between sulfur

20
Q

How many amino acids are there?

A

20

21
Q

What forms amino acid?

A

Amino, carboxyl group
Specific side chain

22
Q

What form are natural amino acids in?

A

L

23
Q

What form are sugars in?

A

D

24
Q

What determines the charge on aa?

A

pH
Carboxyl- negative
Amino- positive

25
Q

What bond forms between amino acids?

A

Peptide
Condensation reaction- release water

26
Q

Properties amino acids?

A

Stable
Cleaved protease/peptidase
Partial double bonds
Flexibility around C

26
Q

Properties amino acids?

A

Stable
Cleaved protease/peptidase
Partial double bonds
Flexibility around C

27
Q

Definition of catalyst?

A

Provide alternative reaction pathway with lower activation energy
Bind to reactants- convert to products

28
Q

Define phosphorylation?

A

Turn enzyme on

29
Q

Define isoenzyme and coenzyme?

A

Isoenzyme- different structure and seq but
catalyse same reaction
Coenzyme- help enzymes cant catalyse alone
- bind with enzyme protein form
active enzymes