DNA & Proteins Flashcards
What are living things made out of?
All living things are made out of proteins or products of proteins
state what proteins are made out of and state their function
- made out of amino acids
- function: determine the structure and function of a cell
Describe the following 4 types of functional proteins in terms of function and description
enzyme
hormone
receptor
antibodies
Enzyme
function: Catalyse chemical reactions
description: Shape of enzyme active site is complementary to the shape of the substrate
Hormone
function: Pass on chemical messages
description: Shape of hormone is complementary to the shape of the receptor protein (on the surface of a cell’s cell membrane)
** Receptor **
function: Receive chemical messages
description: Shape of the receptor protein is complementary to the shape of the signalling molecule or protein
Antibodies
function: Target and recognise foreign cells
description: Shape of antibody is complementary to the shape of the antigens on the surface of foreign cells
Describe the induced fit model
- Enzyme has an active site that is complementary in shape to substrate
- Complementary binding b/w enzyme and substrate
- Enzyme active site changes shape slightly to best fit substrate
- This strains the bonds b/w substrate to reduce activation energy
- Breakdown or synthesis reaction is carried
6, Enzyme remains unchanged to catalyse another reaction
Describe pH affect on enzyme activity
Enzyme work/function best at their optimum pH. Thus, returning pH closer to optimum will increase enzyme activity/function
Change (increase or decrease) in H+ concentrations (in other words pH) will disrupt the weak bonds in tertiary structure; hence this will change the shape of the enzyme active site, hence making it no longer complementary to substrate
- Structural change is temporary
describe effect of Concentration of substrate on enzyme activity
Increase in substrate concentration will increase number of substrates available to partake in the reaction, this increases the chances of successful collisions b/w enzyme and substrate, thus increasing the frequency of complementary binding b/w enzyme and substrate
This consequently increases enzyme activity hence rate of reaction
The rate of reaction is limited by the number of enzymes available
- There is a certain point in time, where all enzyme active sites will be occupied, hence increasing substrate conc. will not increase enzyme activity and rate of reaction will remain constant
Concentration of enzyme effect on enzyme activity?
increase in enzyme concentration will increase the number of active sites available, this increases the rate of successful collisions b/w enzyme and substrate, consequently increasing frequency of complementary binding b/w enzyme and substrate, this increases enzyme activity hence rate of reaction
Enzyme activity is limited by the number of substrates available
- Increasing enzyme concentration will not increase rate of reaction
- Rate of reaction will decrease once all substrates (reactants) have been turned into products
Temperature effect on enzyme activity
Increase in temperature to the optimum, increases particles kinetic energy, consequently increasing the chances of successful collisions b/w enzyme and substrate. This increases the frequency of complementary binding b/w enzyme and substrate, hence increasing enzyme activity hence rate of reaction
Increase pass optimum temperature disrupts the weak hydrogen bonds in secondary, tertiary, and quaternary structure, this permanently changes the shape of the enzyme (denatured) hence the enzyme active site no longer complementary to the substrate, this prevents the substrate from binding. Consequently, no complementary binding b/w enzyme and substrate can occur, therefore rate of reaction and enzyme activity decreases
Inhibitor effect on enzyme activity
**Competitive inhibitor **
- Similar shape to substrate hence it is complementary in shape to enzyme active site
- Binds to enzyme active site to prevent substrate from binding
- Hence, decreases enzyme activity and rate of reaction
**Non-competitive inhibitor **
- Binds to the alternative site (allosteric site) on the enzyme
- This changes the shape of the enzyme active site, making it no longer complementary to the substrate
- Substrate is unable to bind, hence enzyme activity and rate of reaction decreases
What is the function of DNA?
Store and transmit genetic information
State why it is possible for genes in a different type of cell to function in another organism?
DNA is universal in almost all living things – it functions the same
Describe features of the structure of the DNA molecule.
Double stranded helix structure
Nucleotides – that join via complementary base pairing
Sugar-phosphate backbone
What is a gene and what’s its function??
A gene is a section of DNA with a unique base sequence that is the code for synthesis of RNA molecule or RNA molecule that gets turned into a protein
Describe the process of DNA replication
- Helicase unwinds DNA and breaks the hydrogen bonds holding the nucleotides together
- DNA molecule is separated into 2 strands, each strand act as templates
- DNA adds/binds free-floating DNA nucleotides to exposed bases on template DNA strands via complementary base pairing
- DNA polymerase joins the sugar phosphate backbone of DNA nucleotides, synthesising a new strand
- Thus, 2 DNA molecules are formed
Each has 1 strand from the original strand, 1 strand from the newly synthesised strand
State where transcription occurs and describe its process
occurs in: nucleus
- At a specific gene
- Helicase unwinds DNA and hydrogen bonds are broken to separate strands into 2 single strands
- only 1 strand acts as template
- Free floating RNA nucleotides bind to exposed bases on template strand via complementary base pairing
- RNA polymerase joins nucleotides into RNA strand
- DNA rejoins
State where splicing occurs and describe it process
where: cytoplasm
- Removal of introns from primary RNA strand
- Joining of exons to form mRNA strand
state where translation occurs and describe its process
where: cytoplasm at the ribosome
- mRNA binds to ribosome
- Ribosome reads 1 codon (3 mRNA bases)
- tRNA carry amino acid corresponding to anticodon
- tRNA with anticodon complementary to mRNA codon binds via complementary base pairing
- tRNA adds/deposits amino acid to polypeptide chain in correct order
- Process repeats until full protein is formed