Module 2: Foundations In Biology - Biological Molecules Flashcards
In a protein, what are the 4 main elements??
Carbon
Hydrogen
Oxygen
Nitrogen
How many different types of amino acids are there??
20
What is the smallest amino acid??
Glycine
What is the R group of Glycine??
Hydrogen
What is the R group of Cysteine
CH2-SH
What does an R group determine??
Determines properties and bonds that the amino acids form
Hydrophobic
Water repellent
Hydrophyllic
Water loving
Peptide bonding
Two amino acids joined in a condensation reaction
The bond between them is a peptide bond
What is a peptide bond formed between??
Amino acids
What is the resulting compound of peptide bonding??
A dipeptide
In peptide bonding when do the amino acids join??
Amino acids join when the amine and carboxylic acid groups connected to the central carbon atom react
What happens to the hydroxyl in the carboxylic acid group during peptide bonding??
The hydroxyl in the carboxylic acid group of one amino acid reacts with a hydrogen in the amine group of another amino acid
When is a polypeptide formed??
When many amino acids are joined together by peptide bonds
When a polypeptide is formed what is the reaction catalysed by??
Catalysed by the enzyme peptidyl transferase
Where can the enzyme peptidyl transferase be found??
In ribosomes
What is the structure of proteins??
Proteins consist of one or more polypeptides arranged as complex macromolecules
All proteins contain the elements carbon, hydrogen, oxygen and nitrogen
What do many bonds lead to (structure of proteins))
Different types of bonds are formed and these bonds lead to the formation of long chain amino acids
These long chain amino acids fold into complex structures
What is the effect of having different sequences of amino acids??
Leads to different structures with different shapes being produced
Why are shape specific proteins important??
Because the specific shapes of proteins are vital for the many functions proteins have within organisms
Primary protein structure
A sequence chain of amino acids
Which bonds are present in the primary protein structure??
Peptide bonds
Secondary protein structure
Hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern
Which bonds are present in the secondary protein structure??
Hydrogen bonds
Tertiary protein structure
Three dimensional folding pattern of a protein due to side chain interactions
What bonds are present in the tertiary protein structure??
Hydrogen bonds
Ionic bonds
Disulfide bonds
In cysteine what are disulfide bonds formed between??
Formed between two sulphurs
Quaternary protein structure
Protein consisting of more than one amino acid chain
Which bonds formed in the quaternary protein structure??
Hydrogen bonds
Ionic bonds
Disulfide bonds
Hydrophobic/hydrophilic interactions
If the order of amino acids change what happens to the primary structure of the protein??
Primary structure changes
Gives a different function
Where will the bonds be to maintain the quaternary structure??
Between polypeptide chains
Hydrophilic interactions in the middle of the structure
Ionic bonds
Form between positively and negatively charged groups
How can ionic bonds be broken??
By high temperature or a change in ph
What are Disulphide bridges/bonds formed between??
Form between two cysteine amino acids
Disulphide bonds/bridges
Involves sharing electrons so is a covalent bond
Properties of a Disulphide bridge/bond
Strong bond, not broken by an increase in temperature or change in pH
Why do hydrophobic amino acids repel water??
They have non polar R groups
Which way will hydrophobic amino acids face??
Face into cytoplasm or tissue fluid
So will face inwards
Interact and cluster
Why do hydrophilic amino acids love water??
Because they have polar R groups
Which way will hydrophilic amino acids face??
Will face outwards into the tissue fluid or cytoplasm
What do hydrogen bonds form between??
Form between an electropositive H+ atom and an electronegative O- atom
How can hydrogen bonds be broken??
Can be broken by a high temperature or change in pH
Structure of a globular protein
Protein curls into a ball
Hydrophobic R face in
Hydrophilic R face out
Soluble
Structure of a fibrous protein
Proteins form long strands
Insoluble
Very tough
Catalytic example of a globular protein
Enzymes such as amylase and lipase
Regulatory example of a globular protein
Hormones such as insulin
Transport example of a globular protein
Haemoglobin
Protective example of a globular protein
Antibodies
Structural example of a fibrous protein
Collagen
Structural example of a contractile protein
Actin, myosin
What is a prosthetic group??
A prosthetic group is a non-protein part which is permanently bound to the protein and is essential for its purpose
Structure of haemoglobin (globular protein)
2 identical chains called alpha chains
2 identical but different chains called beta chains
Chains packed closely together