Bio Mols Proteins Flashcards
(26 cards)
What 4 elements do proteins contain
Carbon Hydrogen Oxygen Nitrogen Sometimes sulphur
What is the monomer sun Inuit of proteins
Amino acids
How many proteins are commonly occurring in all living organisms
20
What two groups do amino acids always have?
What group differs in amino acids?
Amino agouti NH2
Carboxylic acid group COOH
Differ in the atomic group R
Amino acids are joined by what reaction?
What bond?
What’s the formulae of the bond
Condensation
Peptide bond COHN
Two amino acids join to form a
Dipeptide
Many amino acids join together in a chain to form
Polypeptide
What does a protein consist of
One or more polypeptides
What is the general structure of an amino acids
H. R. Double bond O
N. C. C
H H OH
What is the amino acids formulae
NH2
What is the carboxylic acid formula
COOH
How can proteins be hydrolysed
Heating with acid
Using the enzyme proteases at the optimum temp
How do proteins vary 3
Number and type and sequence of amino acid
How are proteins classified
Occurring to their structure
What is the primary structure of a protein 3
Sequence of amino acids
Joined by peptide bond
On polypeptide chain
What does the sequence of amino acids determine
The specific shape of the protein
What does the secondary structure refer to? Why? What bonds form? Between where? 5 What structures?
The folding or
Coiling
Of the polypeptide chain as a result of hydrogen bonding between the amino acids
Alpha helix or beta pleated sheet
What is the tertiary structure
What does this determine in enzymes
Further coiling and folding of secondary structure due to
Hydrogen Ionic and Disulfude bridges
Determines the shape of the active site and its precise function in enzymes
What two types of tertiary proteins are thee
Globular
Fibrous
What is a globular protein?
Example 2
Are they soluble
Do they have a specific structure
( from alpha helix)
Highly folded and coiled polypeptide chain to produce compact and complex tertiary structure.
Eg enzymes and antibodies
Soluble and have specific structure
What is a fibrous protein structure
Are they soluble
What is their function
Eg
(From beta pleated sheet)
Long and thin and insoluble
Structural functions
Eg keratin in hair
Collagen in tissue
What do quaternary structure relate to?
Which bonds?
Eg
Complex protein consisting of more than one polypeptide chain
Ionic bonds, hydrogen bonds, disulfide bridges and hydrophobic interactions
Proteins will behave similarly to phospholipids in water; the polar groups will form favorable interactions on the surface with water, while the hydrophobic groups will be in the core and away from the water molecules. Usually, amino acids with non-polar residues will be found in the core of proteins.
What is denaturation of proteins
Altercation in the tertiary structure of a protein
Often irreversible of the 3D shape and is no longer functional
What is denaturation usually caused by?
What can cause this? 3
Which bonds are not broken at the temperature?
Breaking hydrogen and ionic bonds
Disulfide bonds
High temperature
Extreme change in pH
Heavy metals