1.3 - Proteins Flashcards
Explain briefly what proteins are
A diverse group of large complex polymers made up of amino acids (after water, they are the most abundant molecules in the body)
What type of functions do proteins have? (hint - there are 5)
- Structural
- Catalytic
- Signalling
- Transport & storage
- Defense
What is the structural function of a protein?
Proteins are the main component of body tissues (e.g muscle, skin, ligaments & hair)
What is the catalytic function of a protein?
All enzymes are proteins, catalysing many biochemical reactions - used for speeding up certain chemical reactions
What is the signalling function of a protein?
Many hormones & receptors are proteins
What is the transport & storage function of a protein?
Proteins are a major element in the transport & storage of certain molecules
What is the defense function of a protein?
Protection against disease - all antibodies are proteins
Name the main parts in the general structure of a protein
- Amino group
- Carboxyl group
- Side chain a.k.a R group (only part of an amino acid that differs between each - defines an amino acid)
Describe how a peptide bond is formed
- From a condensation reaction
- The -OH from carboxyl group of one amino acid & -H from the other amino acid’s amine group
- Form covalent (peptide) bond
- Release a water molecule
Name the structural order of proteins
Primary structure -> Secondary structure -> Tertiary structure -> Quaternary structure
Describe the primary structure of a protein
- unique sequence of amino acids
- determined by inherited genetic info
Describe the secondary structure of a protein
- Found in most proteins
- Consists of coils & folds in the polypeptide chain from H bonding between parts of the polypeptide backbone
Name the two types of secondary structure of a protein
- Alpha helix (coiled)
- Beta pleated sheet (folded)
Describe the tertiary structure of a protein
- Elements of secondary structure come together to form a 3D fold
- Overall shape of a polypeptide, results mainly from interactions between R groups
- Interactions include: H bonds, ionic bonds, hydrophobic interactions, Van Der Waals interactions & disulphide bridges
What are disulphide bridges?
Strong covalent bonds that may reinforce protein structure
Describe the quaternary structure of a protein
When two or more polypeptide chains form one subunit
Name two common examples of proteins that have quaternary structure
- Collagen
- Haemoglobin
Name the 5 factors that affect the protein structure
- Primary structure
Physical & chemical conditions e.g:
- Changes in pH
- Salt concentration
- Temperature
- Other environmental factors that can cause protein to unravel
What does it mean when a protein has denatured?
- The protein has lost its original structure & has become biologically inactive
Describe the general structure of a globular protein & how this affects its function
- Usually have a spherical shape caused by tightly folded polypeptide chains
- Chains are usually folded so that hydroPHOBIC groups are on the INside, while hydroPHILIC groups are in the OUTside
- This allows many of them to be soluble in water
What are the 3 main functions of globular proteins?
Transport:
- Proteins
- Enzymes
- Hormones
Give an example of a globular transport protein & where they are found
- E.g haemoglobin & myoglobin
- These proteins are embedded in membranes
Give an example of a globular enzyme
- Lipase
- DNA polymerase
Give an example of a globular hormone
- Oestrogen
- Insulin