Primary Structure The sequence of amino acids in the polypeptide chain
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03.05.2018
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Primary
Structure -
The sequence of amino acids in the polypeptide chain
Primary Structure -
The sequence of amino acids in the polypeptide chain
Secondary Structure -
The formation of helices and pleated sheets due to hydrogen bonding
between the peptide backbone
Tertiary Structure -
Folding of helices and sheets
influenced by R group bonding
Quaternary Structure -
The association of more than one polypeptide into a protein complex influenced by R group bonding
The peptide backbone has areas of positive charge and negative charge
The peptide backbone has areas of positive charge and negative charge
These areas can interact with one another to form hydrogen bonds
The result of these hydrogen bonds are two types of structures:
helices
pleated sheets
Tertiary structure results from the folding of helices and pleated sheets
Tertiary structure results from the folding of helices and pleated sheets
Factors influencing tertiary structure include:
Hydrophobic interactions
Hydrogen bonding
Disulphide bridges
Ionic bonds
e.g. haemoglobin
e.g. haemoglobin
3º structure
normally folds up in a ball
hydrophilic R groups point outwards
Hydrophobic R groups point inwards
soluble
metabolic functions
Collagen is a fibrous protein made of 3 polypeptide helices held
together by hydrogen bonding
Collagen is a fibrous protein made of 3 polypeptide helices held together by hydrogen bonding
Every 3rd amino acid in the chain is a glycine (very small to let the chains lie close to each other)
Collagen molecules are found side by side forming fbres
The staggered ends help to give collagen fibres great tensile strength
Quaternary structure results from the interaction of
independent polypeptide chains
Quaternary structure results from the interaction of independent polypeptide chains
Factors influencing quaternary structure include:
Hydrophobic interactions
Hydrogen bonding
The shape and charge distribution on amino acids of associating polypeptides
Haemoglobin is a globular protein with a prosthetic ‘iron’ group
Haemoglobin is a globular protein with a prosthetic ‘iron’ group
In adults, hemoglobin is made up of 4 polypeptides (2 polypeptide chains and 2 polypeptide chains)
Each polypeptide surrounds a prosthetic ‘haem’ group
Hydrophobic interactions between side groups pointing
inwards maintain the structure
Hydrophilic side chains point outwards making it soluble
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