1. biological molecules

4 common elements in biological molecules

carbon, hydrogen, nitrogen and oxygen

what are monomers usually based on

carbon

in hydrogen bonding what part of the water molecule has a negative charge

oxygen

what does a condensation reaction produce

water

what reaction must occur in order to form a monomer from a polymer

condensation

What are monosaccharides known as

simple sugars

general formula of monosaccharides

(CH20)n

glucose formula

C6H12O6

Two types of glucose

alpha and beta

what do alpha glucose molecules combine to form

starch and glycogen

what do beta glucose molecules combine to form

celloluse

3 reducing sugars

glucose, galactose and fructose

2, 5 carbon hexoses

fructose and galactose

6 carbon pentose

deoxyribose

what do 2 monosaccharides combine to form

disaccharide

what bond links the 2 subunits between sugars

glycosidic bonds

glucose + glucose forms

maltose

glucose + galactose forms

lactose

glucose + fructose forms

sucrose

long chains of monosaccharides form

polysaccharides

is starch insoluble or soluble?

insoluble

what is starch a mixture of?

amylose and amylopectin

why is the digestion of amylopectin quicker than amylose

have more intramolecular hydrogen bonds, more branches which can be broken

where is cellulose found

only plants

test for reducing sugars and non reducing sugars

benedicts test

What does Benedict's solution reduce

copper II ions to copper I ions

3 ways cellulose gives strength

long unbranched chains, which run parallel to one another and form hydrogen bonds between them

what do the cellulose molecules group to form

microfibrils

how many carbon atoms does a fructose molecule have

6

what are cellulose molecules made by

condensation reactions

What are triglycerides formed by

condensation reactions

What is a tryglyceride composed of?

1 glycerol and 3 fatty acids

what are lipids used as

insulation and as an energy store

what do lipids contain

carbon, hydrogen, oxygen

what are lipids soluble in

organic solvents ie alcohol and acetone

2 main groups of lipids

triglycerides and phospholipids

what low ratio do triglycerides have

low mass to energy ratio

what do triglycerides produce when oxidised

water

What makes triglycerides insoluble in water?

hydrophobic tails

what makes a fatty acid unsaturated

double bond between two carbon atoms

a long chain of of carbon atoms in a fatty acid means that it is

hydrophobic

phospholipid is made up of

2 fatty acids and a glycerol

phosphate group is (to do with water)

hydrophilic

test for lipids

Emulsion test - ethanol and water shaken

what are the C=O bonds

ester bonds

what is the cell wall made of

murin

what does hydrolysis of a lipid produce

fatty acids

what do proteins function as

enzymes, hormones and oxygen transporters

what do proteins form to make

skin, hair, feathers and nails

How many naturally occurring amino acids are there?

20

2 amino acids form to make

a dipeptide

what bond does the formation of a dipeptide produce

peptide bond

what shape do individual amino acids show

tetrahedral

what is the name of the simplest amino acid

glycine

what is the r-Group for the simplest amino acid

hydrogen atom

the 2 sulfur containing amino acids

cysteine and methionine

what bonds hold amino acids together

peptide bonds

What is the primary structure of a protein?

the number, type and sequence of amino acids

what does the primary structure determine

the proteins function in the end

the three parts of the generalised structure of amino acids

amino group(basic), r- group, carboxyl group (acidic)

how is the secondary structure of a protein formed

weak negatively charged nitrogen and oxygen atoms interact with the weak positively charged hydrogen atoms, forming hydrogen bonds

whats released in a condensation reaction

water

what should you look for when identifying a peptide bond

where nitrogen is bonded to a carbon which as a double bond with oxygen

two structure of secondary proteins

alpha helix and beta pleated sheets

why are beta pleated sheets formed

the protein folds so that two parts of the polypeptide chain are parallel to each other, enabling hydrogen bonds to form between them

why does the alpha helix form

the amino acid chain coils into a right- handed helix and hydrogen bonds form between between the oxygen and hydrogen atoms that have been brought together

how is the tertiary structure formed

after secondary structures have formed, the molecule bends and folds into a 3-D globular shape

all globular proteins display what type of structure

tertiary

give an example of a globular protein and where its found

myoglobin, found in muscle cells

what are the hydrogen bonds between in tertiary structures

the r groups

what are the hydrogen bonds between in secondary structures

amino and carboxyl groups

What is tertiary structure?

3d folding of polypeptide chain due to hydrogen and disulphide bonds

way's starch has adapted for its function in plant cells

insoluble - doesn't affect water potential

what is quaternary structure

two or more polypeptide chains

what reaction forms proteins

condensation

2 examples of quaternary proteins

haemoglobin and collagen

what does every amino acid possess

an amino end and a carboxyl acid end

what stabilises the secondary structure of proteins

hydrogen bonds

what do the pockets formed by tertiary structure hold

substrates

what's the name of the pockets formed by tertiary structure

active sites

what is cellular metabolism

the sum of all the reactions carried out out by cells

2 types of metabolic reactions

catabolic and anabolic

catabolic reaction

substance breakdown and release energy

anabolic reaction

chemical reactions take in energy to synthesise complex molecules from simple molecules

what are catabolic reactions in terms of energy

exergonic - give out energy

what are anabolic reaction in terms of energy

endergonic - take in energy

induced fit model

when the substrate enters the active site it induces a change in the shape of the enzyme - enables an enzyme - substrate complex

name of a protein that contains a non amino part

conjugate protein

name of the non amino group on the protein

prosthetic group

intracellular enzymes

produced and function inside the cell

extracellular enzymes

secreted by cells and catalyse reactions outside cells

example of catabolic reactions

cellular respiration and hydrolysis

examples of anabolic reactions

protein synthesis and photosynthesis

what type of proteins are enzymes

globular

why does a lower temperature slow the rate of reactions

less successful collisions between substrate and active site, collide with less energy

equation for pH

-log10(H)

what do competitive inhibitors bind to

the active site of the enzyme

what do non competitive inhibitors bind to

the enzyme at a position other than the active site

What are competitive inhibitors?

Molecules that bind to the active site of an enzyme and inhibit the ability of the substrate to bind.

What are non-competitive inhibitors?

bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective