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Biomolecule Flashcards

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AP® Biology flashcards Biology 101 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
Q

How is triglycerides made

A

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
Q

Properties of saturated triglycerides

A

No Carbon- carbon double bond

Melting point high

State rtp solid

Example butter

27
Q

Properties Unsaturated triglycerides

A

Have carbon carbon double bond

Low melting point

State rtp liquid

Example oil

28
Q

How is a liquid triglycerides

A

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
Q

Describe amino acid

A

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
Q

Polypeptide

A

Two or more amino acid joined together

31
Q

Dipeptide

A

Two amino acid joined by peptide bonds

32
Q

Primary structure of protein

A

Sequence of amino acid in a protein held together by peptide bond

33
Q

Secondary structure of protein

A

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
Q

Tertiary structure in protein structure

A

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
Q

Quaternary structure in protein

A

A specific 3D shape of a protein that is determined by multiple polypeptide chains held together by hydrogen , ionic, disulphide bonds

36
Q

Globular proteins 3D structure

A

Complex tertiary and sometimes quanternary structure and fold into spherical (globular) shapes

37
Q

Globular protein properties

A

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
Q

Haemoglobin

A

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
Q

What is fibrous

A

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
Q

Collagen structure and properties

A

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
Q

Define Conjugated protein

A

Protein molecule joined with or conjugated to prothetic group

42
Q

Define prosthetic group

A

A molecule incorporated in a conjugated protein

43
Q

Lipoprotein

A

Proteins conjugated with lipids prosthetic group

—> help transport of cholesterol in blood

44
Q

Glycoprotein

A

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
Q

Principle of circulation

Transport in small organism

A

Very small distance

Surface area to volume ratio is large

Low metabolic demand need less nutrients O2 excrete less waste

46
Q

Tranport in large organism

A

Small surface area to volume ratio is small

High metabolic rate

Diffusion alone isnt enough

Transport oxygen and heat using mass flow

47
Q

Double circulation system advantages

A

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
Q

Arteries

A

-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
Q

Vein

A

Smooth muscle

  • control /maintain blood flow
  • contract pushing blood along
50
Q

Capillaries

A

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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