Functional group of amino acids
Carboxylic and amine group
At normal PH of body fluids, these groups are ionised
What are proteins
large organic molecules containing carbon, nitrogen, oxygen, hydrogen
What is the R group
The side chain of the amino acid that gives the amino acid a distinctive chemical property
Types of proteins
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S = structural
R = regulatory (neurotransmitters ,hormones for growth)
C = contractile (shortening of muscle fibres)
I = immunology
T = transport
C = catalytic
What are the ‘special’ amino acids
Glyciene = simplest amino acid with only a H in its side chain
cysteine = Has sulfur in its side group
Tyrosine = has six carbon ring in its side chain
Lysine = seond amino group in its side chain
How do amino acids bond together
Peptide bond forms in a condensation reaction between the carbon in the carboxyl group and nitrogen in the amino group
How are different proteins created
There are 20 amino acids, the different arrangement of amino acids in a polypeptide chain creates a different protein as different R group at diff position so diff bonding occurs
Primary structure of protein
amino acid sequence genetically determined by cell DNA
Secondary structure
Polypeptide becomes 2D as hydrogen bonds form between the O from carboxyl group and H from amino group.
Alpha helix = between every 4th amino acid
Beta pleated = between parallel chains
Tertiary structure
Each proteins tertiary structure is unique and determines how protein will function
Bonds are from R group interactions
What bonds are in tertiary structure
Disulfide (covalent) - between cysteine amino acids
Weak H bonds
Ionic bonds
Hydrophobic interactions
what are hydrophobic interactions
amino acids with hydrophobic R group will fold into the central core while amino acids that have hydrophilic R groups will be at the surface.
quaternary structure
Forms in proteins that consist of more than one polypeptide
Bonds are similar to the ones that are in tertiary structure
fibrous proteins
Insoluble
Made of long chains lined parallel to each other
Structural functions
Globular
Spherical and soluble
Metabolic functions
what is denaturisation
Environmental changes causes protein to unfold and lose its characteristic shape, however, denaturisation can sometimes be reversed