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Biology-Corinna > 1.Biological Molecules > Flashcards

1.Biological Molecules Flashcards

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1
Q

What is a
Covalent bond
Ionic bond
Hydrogen bond

A

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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2
Q

What is polymerisation

A

Joining up of monomers to form polymers

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3
Q

What is a

Condensation reaction

Hydrolysis reaction

A

Removal of water to join monomers

Addition of water to split up polymers

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4
Q

What are carbohydrates made of

What’s a monosaccharide

What’s a disaccharide

A

Oxygen carbon hydrogen oxygen nitrogen

Individual building block of carbs

Pair of monosaccharides joined by a glycosidic Bond

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5
Q

What are the two isomers of glucose

A

Alpha glucose (down up down down)

Beta glucose (down up down up)

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6
Q

What is the test for reducing sugars

A

Heat Benedictus reagent with solution

Goes orange/brown

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7
Q

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

A

Condensation reaction and glycosidic bond

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8
Q

What Are the monomers that form

Maltose
Sucrose
lactose

A

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

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9
Q

What’s the test for non reducing sugars

A

Heat with hydrochloride acid

Then heat with Benedictus solution

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10
Q

Why do you heat a non reducing sugar with HCL

A

To split up the disaccharides

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11
Q

What’s a polysaccharide

A

Many disaccharides joined together through condensation reactions

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12
Q

Facts about starch

A

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

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13
Q

What’s the role of starch

A

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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14
Q

What’s the test for starch

A

Add iodine solution and it’ll go blue/ black

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15
Q

Facts about glycogen

A

Found in animals and bacteria
Shorter chains
Very branched
Small granules

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16
Q

What’s the role of glycogen

A

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

17
Q

Structure of cellulose

A 
B glucose
Straight chains
Chains run parallel
Hydrogen bonds between chains
Macrofibrils, macrofibrils, cellulose
Cross bridging
18
Q

What’s the function of cellulose

A

Cell walls
Prevents cells from bursting
Exerts inwardly pressure

19
Q

How is cellulose suited to function

A 
Long straight unbranched chains
Cross linked 
Add strength 
Rigid 
Fibres grouped together add strength
20
Q

Facts about lipids

A

Contain oxygen carbon hydrogen
Insoluble in water
Soluble in organic solvents

21
Q

Role of lipids

A 
Cell membrane-fluidity/flexibility
Source of energy-if oxidised more energy than carbs 
Water proofing-waxy cuticles 
Insulation-slow conductors 
Protection-organs
22
Q

What forms a triglyceride?

What’s the bond an reaction

A

3 fatty acids and glycerol

Joined in condensation reaction to form Ester bond

23
Q

How is triglycerides structure related to function

A

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

24
Q

Facts about phospholipids

A

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

25
Q

How is phospholipids structure related to function

A

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

26
Q

What’s the test for lipids

A 
Add ethanol
Shake
Add cold water
Shake
Goes cloudy
27
Q

What are amino acids made of

What’s the bond that joins them together

A

Carboxyl group, amine group and R-group

Condensation raacion to form peptide bond

H     H      O
    \    I       /
    N -C -C
   /     I     \
H     R     OH
28
Q

What is the primary structure of a protein

A

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

29
Q

What’s the secondary structure of a protein

A

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

30
Q

Whay happens in the tertiary structure of proteins

A

R groups of amino acids bond together to give a more complex 3D shape

Disulphides bridges
Ionic bonds
Hydrogen bond
Hydrophobic interactions

31
Q

What happens in the quarternary structure

A

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

32
Q

What’s the test for proteins

A

Add biuret reagents

Purple colour=protein

33
Q

Facts about enzymes

A

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

34
Q

What’s the structure of enzymes

A

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

35
Q

What effect does temperature have on enzyme action

A 
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

36
Q

What’s the effect of oh on enzyme action

A

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

37
Q

Effect of enzyme conc on enzyme action

A

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

38
Q

YEffect f substrate conc on enzyme action

A

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

39
Q

What’s an enzyme inhibitor?

What are the two types of inhibitor

A

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

Biology-Corinna (22 decks)

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