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Biomolecule Flashcards

1
Q

Describe the structure of a water molecule

A
  • one oxygen atom covelently bonded to two hydrogen atoms

- oxygen is more electronegative than hydrogen which leads to polar bonds and an uneven charge distribution

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2
Q

What is a hydrogen bond

A

Strong intermolecular forces

Hydrogen atoms which are directly covalently bonded to a highly electronegatively atom (NOF) are attracted to highly electronegative atoms in other molecule

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3
Q

What is a solvent

A

Any substance which solutes can dissolve in to form a solution

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4
Q

State 6 important properties of water

A
  • act as a solvent
  • act as a metabolite
  • high surface tension
  • high specific heat capacity
  • high latent of vaporisation
  • strong cohesion and adhesion forces
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5
Q

Why is cohesion useful in biological systems

A

Cohesion is the main force supporting columns of water as they are pulled up the xylem in plants. The water molecules stick together as a constant column

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6
Q

Why is adhesion useful in biological system

A

It allows water to move against the pull of gravity up the xylem

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7
Q

What are carbohydrates

A

Molecules that consists of carbon, hydrogen and oxygen only

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8
Q

What are monosaccharides

A

One sugar unit

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9
Q

What is a disaccharides

A

When two monosaccharides covalently linked by glycosidic bond by condensation reaction

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10
Q

What is a polysaccharides

A

A polymer made of many monosaccharides covalently linked by glycosidic bond

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11
Q

Properties of monosaccharides

A

Single sugar unit

Water soluble

Taste sweet

Reducing

Single-ring structure

No glycosidic

Osmotic effect

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12
Q

Disaccharides

A

Water soluble

Taste sweet

Reducing ( not sucrose)

Two ring structure

Glycosidic

No osmotic effect

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13
Q

Polysaccharides

A

Insoluble

Not sweet

Non-reducing

No osmotic effect

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14
Q

Define isomers

A

Same molecular formula but different structure formula

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15
Q

Describe what happens in a condensation reaction

A

Two molecules are joined togther and water is removed

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16
Q

What type of reaction breaks a glycosidic bond

A

Hydrolysis reaction

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17
Q

Describe what happens in a hydrolysis reaction

A

A molecule is broken apart using water

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18
Q

Describe the structure of glycogen

A

Made up of alpha glucose molecules joined by either alpha 1,4 or alpha 1,6 bonds

Highly branched

Compact

Large molecule - store lots of energy

Insoluble - no osmotic effect

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19
Q

Function of glycogen

A

Main energy storage material in animals

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20
Q

Describe the structure of starch

A

Made up amylose (joined by alpha 1,4 bomds)

  • unbranched
  • coiled
  • compact -can fit more glucose molecules in a small space

Amylopectin (joined 1,4 and 1,6 alpha bonds)
-branched chain - can be rapidly hydrolysed by enzyme break down into glucose to be released

Starch is also insoluble in water - so it doesnt cause water to enter cells by osmosis
-good for storage
-
-

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21
Q

Sucrose monosaccharides

A

Glucose + fructose

Stored in plants such as sugar cane

22
Q

Lactose monosaccharides

A

Glucose + galactose

Milk sugar - main carbohydrates found in milk

23
Q

Maltose monosaccharides

A

Glucose + glucose

Malt sugar - found in germinating seed such as barley

24
Q

What 3 element are triglycerides made up of

A

Carbon hydrogen and oxygen

25
How is triglycerides made
Triglycerdies are formed by condensation of 1 glycerol molecule and 3 fatty acids forming an ester bond between the carboxyl and hydroxyl group releasing 3 molecules of water
26
Properties of saturated triglycerides
No Carbon- carbon double bond Melting point high State rtp solid Example butter
27
Properties Unsaturated triglycerides
Have carbon carbon double bond Low melting point State rtp liquid Example oil
28
How is a liquid triglycerides
The different state due to the presence of a double bond between carbon atoms in the fatty acids tail —> double bond cause the bend pushes the unsaturated triglycerides molecule further apart than the saturated molecules —> this weakens the intermolecular forces between the unsaturated triglycerides molecule so they form a liquid
29
Describe amino acid
Building blocks of protein consisting of an amino group (-NH2) and carboxyl group (-COOH) attached to a carbon atom and R group that varies between amino acid
30
Polypeptide
Two or more amino acid joined together
31
Dipeptide
Two amino acid joined by peptide bonds
32
Primary structure of protein
Sequence of amino acid in a protein held together by peptide bond
33
Secondary structure of protein
Is the folding of the polypeptide chain into alpha helices and beta-pleated sheets due to the formation of hydrogen bonding -the hydrogen in NH2 is slightly positive and the oxygen in -C=O is slightly negative resulting hydrogen bond between amino acid — alpha helix the polypeptide chain coils with hydrogen bond keeping rhe coil stable -pleated betasheet chain form a zigzag and fold over themselves
34
Tertiary structure in protein structure
Further folding of the secondary structure to form a unique functional 3D shape held togther by ionic, hydrogen & disulphide bond -alpha helices and beta pleated sheets also twist and turn to form a protein with unique 3D structure
35
Quaternary structure in protein
A specific 3D shape of a protein that is determined by multiple polypeptide chains held together by hydrogen , ionic, disulphide bonds
36
Globular proteins 3D structure
Complex tertiary and sometimes quanternary structure and fold into spherical (globular) shapes
37
Globular protein properties
Proteins soluble Outer layer - R group is hydrophilic Inner layer - R group is hydrophobic Molecule is so big Forms a colloid Carboxyl and amino acid ends give them ionic properties so might expect them to dissolve in water, form a solution
38
Haemoglobin
Consists of 4 polypeptide chains which are 2 alpha chains and 2 beta chains - each polypeptide chain contains a iron - haem containing group (prothetics group) that bind with oxygen then released when required - soluble, so it can be easily transported - it is a quanternary structure —> has 4 polypeptide 4 haem prothetic groups —> conguagated protein
39
What is fibrous
Little or no tertiary structure Long parallel polypeptide chains with occasional crosslinkage that forms them into fibre Contain large proportion of amino acid with hydrophobic R groups —> insoluble - too large to be dissolve in water Triple helix - high tensile strength
40
Collagen structure and properties
The primary structure of these chain is repeating sequence of glycine with two others Quanternary structure has 3 polypeptide chain The 3 polypeptide alpha - chains are arranged/wrapped around into a unique triple held by hydrogen bond —> help stabilise the quanternary structure Collagen further strengthened by crosslinking between different triple helical molecule
41
Define Conjugated protein
Protein molecule joined with or conjugated to prothetic group
42
Define prosthetic group
A molecule incorporated in a conjugated protein
43
Lipoprotein
Proteins conjugated with lipids prosthetic group —> help transport of cholesterol in blood
44
Glycoprotein
Proteins with a carbohydrates prosthetic group -help in holding lots of water so harder for protein- digesting enzyme (proteases break them down) Lubricants -mucus -synovial fluid in joints —> stomach produces mucus to protect enzyme attack the stomach wall
45
Principle of circulation | Transport in small organism
Very small distance Surface area to volume ratio is large Low metabolic demand need less nutrients O2 excrete less waste
46
Tranport in large organism
Small surface area to volume ratio is small High metabolic rate Diffusion alone isnt enough Transport oxygen and heat using mass flow
47
Double circulation system advantages
Oxygenated and deoxygenated blood cannot be mixed are separated thus maintain a steep concentration gradient Transport at high pressure Transport oxygen at hih pressure using mass flow
48
Arteries
-smooth muscle —> thicker change the diameter of the vessel to control blood flow Elastic fibre - maintain high blood pressure - stretch and recoil Collagen -provides strengthen prevent from rupture Smooth endothelium reduce friction Narrow lumen maintain high blood pressure
49
Vein
Smooth muscle - control /maintain blood flow - contract pushing blood along
50
Capillaries
One cell thick -short diffusion distance Narrow lumen -slow blood flow, red blood cell can only fig through and squeezed against the walls and this maximise diffusion Pores In walls between cells allow substances to escape Red blood cell can only squeezed against the walls maximise diffusion

Biology (27 decks)

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