BIOLOGICAL MOLECULES Flashcards by Elodie Howarth

1.1 How to Hydrogen bonds form?

Attraction between POLAR molecules

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1.1 what are polymers made up of?

MONOMERS linked together to form long chains

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1.1 what is the reaction which produces a polymer called

Polymerisation

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1.1 what happens in a hydrolysis reaction

A molecule of water is produced

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1.1 what happens in a condensation reaction?

A molecule of water is required for the reaction to occur

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1.1 define metabolism

All the chemical processes that take place in living organisms (collectively)

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1.1 what number of particles does one mole of a substance contain?

The same number of particles that there are in 12g of carbon-12 atoms.
Aka 6.022x10^23 (AVOGADROS CONSTANT)

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1.2 What is the most unusual feature of carbon?

They readily form bonds with other carbon atoms

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1.2 what elements are carbohydrates made up of?

Carbon, Hydrogen and Oxygen
(CHO)

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1.2 what are 3 examples of monomers?

Monosaccharides
Amino acids
Nucleotides

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1.2 what is a disaccharide?

2 monosaccharides joined together

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1.2 what is the general formula of monosaccharides?

(CH2O)n
‘n’ can be any number between 3 and 7

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1.2 what is a reducing sugar?

A sugar that can be reduced (gain an electron or gain hydrogen) in a reaction

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1.2 what is the test for reducing sugars?

• BENEDICT’S
• Goes from blue -> orange-brown (usually)
• HEAT in water bath at 85°

(Can also turn green, yellow or red depending on the amount of reducing sugar present. Green being smallest amount and red bring the highest)

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1.2 what are 3 important monosaccharides

• glucose
• fructose
• galactose

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1.3 what is MALTOSE made up of

Glucose + glucose

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1.3 what is SUCROSE made up of

Glucose + fructose

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1.3 what is LACTOSE made up of?

Glucose + galactose

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1.3 what type of reaction occurs when monosaccharides join?

Condensation reaction

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1.3 what is the name of the bond formed when monosaccharides join?

Glycosidic bond

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1.3 what are the steps of the test for non-reducing sugars

• Add dilute HYDROCHLORIC ACID and water bath for 5min to break glycosidic bonds and result in monosaccharides
• neutralise HCl with SODIUM HYDROCARBONATE
• Re-test with BENEDICTS

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1.3 what reaction forms a polysaccharide from monosaccharides

Condensation reaction

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1.3 what is the test for starch?

Study These Flashcards

•IODINE
• orange-brown -> blue-black

1.4 what is starch made up of?
What’s its structure like?

Study These Flashcards

• ALPHA GLUCOSE
- Chains branched or unbranched
- Unbranched chain forms a tight, compact coil

1.4 what bond and reaction links alpha-glucose monomers in starch?

Glycosidic bonds formed in condensation reactions

1.4 what is the main role of starch?

Energy storage

1.4 what cells is starch never found in?

Animal cells

1.4 what is glycogen made up of?

• ALPHA GLUCOSE - shorter chains than starch - More highly branched

1.4 what is cellulose made up of

• BETA GLUCOSE - straight unbranched chains - run paralleled and link chains by H-bonds

1.4 what do cellulose molecules group to form

Microfibrils (Arranged in parallel groups to form fibres)

1.5 what elements do lipids contain

Carbon, Hydrogen and Oxygen (CHO)

1.5 what are triglycerides made up of?

Three fatty acids combined with one glycerol

1.5 in triglycerides, what bond and reaction takes place to bind the fatty acids with the glycerol?

Ester bond Condensation reaction (Hydrolysis therefore separates components)

1.5 what are triglycerides made up of

A carboxyl (-COOH) group A hydrocarbon chain

1.5 what are the 2 main features of phospholipids

• hydrophilic heads • hydrophobic tails (Results in a POLAR molecule)

1.5 what is the test for lipids

- add ethanol - shake - add water Milky white emulsion shows positive test

1.6 what 3 groups are in an amino acid

• amino group (--NH2) • carboxyl group (--COOH) • variable group (represented by R)

1.6 what are the bonds called when amino acid chains join, what is the reaction called?

• peptide bond • condensation reaction

1.6 what is the primary structure of proteins called? How does this structure form?

POLYPEPTIDES - they are a chain of hundreds of amino acids and joined during POLYMERISATION

1.6 what does the primary structure of proteins determine?

The SHAPE of the protein which is very important to its FUNCTION

1.6 how does the secondary structure of proteins form?

Amino acids are POLAR and form weak HYDROGEN BONDS. Causes polypeptide chain to be twisted into a 3D shape

1.6 what are the names of secondary structures of proteins?

Alpha-helix Beta pleated sheet

1.6 what bonds form the tertiary structure of proteins?

• ionic bonds • disulphide bridges -> between carboxyl and amino groups (not involved in peptide bonds) • hydrogen bonds

1.6 what forms the quaternary structure of proteins

• A number of individual polypeptide chains • May also be prosthetic (non-protein) groups

1.6 what is the test for proteins

BIURET TEST: - dilute copper sulphate Positive test indicates presence of peptide bonds Positive: blue -> purple

1.7 what type of proteins are enzymes?

Globular proteins

1.7 what is the function of enzymes

Catalyse a reaction by allowing an alternative reaction pathway and lowering the activation energy of a reaction WITHOUT getting used up in the reaction

1.7 what is the induced model of enzyme action

The idea that enzymes mould around substrates rather than already having a perfect fit

1.8 what ways can you measure the rate of an enzyme catalysed reaction

• measure formation of products • measure disappearance of substrate

1.8 how does temp increase affect enzyme reaction

• increases KINETIC ENERGY • enzymes have an OPTIMUM TEMP • if temp too high or low, enzyme DENATURE and bonds forming the tertiary structure of the enzyme break, meaning it can't function again

1.8 what is the effect of pH on enzyme action

• enzymes have an optimum pH • too drastic of a change will result in damage to tertiary structure and enzyme DENATURING

1.8 how does concentration of enzymes effect a reaction

If there is EXCESS SUBSTRATE, there will be a proportional increase in rate of reaction If substrate is a LIMITING FACTOR, there will be no effect

1.8 what effect will substrate concentration have on an enzyme catalysed reaction

If enzymes are in excess, proportional increase in r.o.r If enzymes limiting factor, no effect

1.9 how do competitive inhibitors work

They compete for a space in the active site and prevent substrates from binding to the enzyme -> preventing the enzyme from catalysing the reaction

1.9 how do non-competitive inhibitors work

They bind to an enzyme somewhere other than the active site and change the shape of the active site of the enzyme

BIOLOGICAL MOLECULES Flashcards

(55 cards)