1.Biological Molecules Flashcards by Corinna Smith

What is a
Covalent bond
Ionic bond
Hydrogen bond

Atoms share pair of electrons in their outer shell-once filled it’s stable

Ions with Opposite charges attract one another-electrostatic atttraction

When S -ve region is attracted to S +ve region of another polar molecule

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What is polymerisation

Joining up of monomers to form polymers

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What is a

Condensation reaction

Hydrolysis reaction

Removal of water to join monomers

Addition of water to split up polymers

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What are carbohydrates made of

What’s a monosaccharide

What’s a disaccharide

Oxygen carbon hydrogen oxygen nitrogen

Individual building block of carbs

Pair of monosaccharides joined by a glycosidic Bond

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What are the two isomers of glucose

Alpha glucose (down up down down)

Beta glucose (down up down up)

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What is the test for reducing sugars

Heat Benedictus reagent with solution

Goes orange/brown

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What’s the reaction and bond that forms when two monosaccharides are joined together

Condensation reaction and glycosidic bond

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What Are the monomers that form

Maltose
Sucrose
lactose

A glucose + A glucose
A glucose + fructose
A glucose + b galactose

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What’s the test for non reducing sugars

Heat with hydrochloride acid

Then heat with Benedictus solution

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Why do you heat a non reducing sugar with HCL

To split up the disaccharides

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What’s a polysaccharide

Many disaccharides joined together through condensation reactions

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Facts about starch

Major energy storage
Most abundant in plants
Small grains
Found in tight coils making it compact

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What’s the role of starch

Energy storage
Insoluble so doesn’t affect water potential, doesn’t diffuse out of cells
Very branched so when hydrolysed quick release of glucose
Easily transported

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What’s the test for starch

Add iodine solution and it’ll go blue/ black

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Facts about glycogen

Found in animals and bacteria
Shorter chains
Very branched
Small granules

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What’s the role of glycogen

Energy storage
Insoluble, doesn’t draw in water
Compact-lots stored in small place
Simultaneously worked on by enzymes for quick release

Structure of cellulose

B glucose
Straight chains
Chains run parallel
Hydrogen bonds between chains
Macrofibrils, macrofibrils, cellulose
Cross bridging

What’s the function of cellulose

Cell walls
Prevents cells from bursting
Exerts inwardly pressure

How is cellulose suited to function

Long straight unbranched chains
Cross linked 
Add strength 
Rigid 
Fibres grouped together add strength

Facts about lipids

Contain oxygen carbon hydrogen
Insoluble in water
Soluble in organic solvents

Role of lipids

Cell membrane-fluidity/flexibility
Source of energy-if oxidised more energy than carbs 
Water proofing-waxy cuticles 
Insulation-slow conductors 
Protection-organs

What forms a triglyceride?

What’s the bond an reaction

3 fatty acids and glycerol

Joined in condensation reaction to form Ester bond

How is triglycerides structure related to function

Insoluble in water-doesn’t affect water potential
High ratio of energy-in carbon/hrdogen bonds
Low mass to energy ratio-lots energy stored in small place

Facts about phospholipids

Hydrophilic head-associates with water
Hydrophobic tail-orients itself away from water

Group of phospholipids heads associate together and with water to form a lipid bilayer or hydrophobic tails

How is phospholipids structure related to function

Bilayer in water-hydrophobic barrier between environment and cell contents Allows formation of glycolipids-cell recognition

What’s the test for lipids

``` Add ethanol Shake Add cold water Shake Goes cloudy ```

What are amino acids made of What’s the bond that joins them together

Carboxyl group, amine group and R-group Condensation raacion to form peptide bond ``` H H O \ I / N -C -C / I \ H R OH ```

What is the primary structure of a protein

Series of condensation reactions amino acids joined in process called polymerisation The sequence of amino acids that forms a primary structure of proteins that determines the shape and function

What’s the secondary structure of a protein

Polypeptide chain twists into either alpha helix or beta pleated sheets due to localised hydrogen bonding

Whay happens in the tertiary structure of proteins

R groups of amino acids bond together to give a more complex 3D shape Disulphides bridges Ionic bonds Hydrogen bond Hydrophobic interactions

What happens in the quarternary structure

More than 2 polypeptide chains are linked and bond together via their R groups Prosthetic groups associate with the molecules (non protein groups)

What’s the test for proteins

Add biuret reagents Purple colour=protein

Facts about enzymes

Catalysts Lower activation energy Need substrate to collide and to have min amount of energy for reaction to occur

What’s the structure of enzymes

Globular proteins Specific shape Active site that’s lined with R groups and amino acids Bonds temporarily with a substrate molecule

What effect does temperature have on enzyme action

``` Rise in temp = increase in kinetic energy Molecules move faster Collisions more frequent More successful collisions More e-s complexes Increase enzyme action ``` Further increase causes hydrogen bonds in enzyme to break Denaturation is permanent shape change of active site-subrate dont fit

What’s the effect of oh on enzyme action

PH is hydrogen ion concentration Each enzyme has own optimum Either side of optimum the reaction slows down Bonds in tertiary structure break and change Active site changes shape Sub rate no longer fit

Effect of enzyme conc on enzyme action

Excess of substrate-increase in number of enzymes will increase the rate of reaction proportionally Limit of substrate-increase in enzymes will increase rate of reaction until no substrate left to work on

YEffect f substrate conc on enzyme action

Enzyme conc fixed-rate of reaction increases in proportion until no more free enzymes left as they become saturated

What’s an enzyme inhibitor? What are the two types of inhibitor

Something that directly or indirectly interferes with the functioning of the active site Competitive-binds to active site instead of substrate, not permanent bonding, the greater the conc of inhibitor the slower the reaction Non competitive-binds to allosteric site, changes shape of enzyme and active site, substrate doesn’t fit, increasing conc of substrate doesn’t decrease effect of inhibitor