Learning outcomes Describe the structure of an amino acid. Describe the formation and breakage of peptide bonds in the synthesis and hydrolysis of dipeptides.
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Learning outcomes• Describe the structure of an amino acid.
• Describe the formation and breakage of peptide bonds in the synthesis and hydrolysis of dipeptides and polypeptides.
The primary structure is just the sequence of amino acids in the polypeptide chain
Proteins
There are a huge number of possible combinations of amino acids that can make up proteins.
A four-amino-acid structure like this has 160,000 (20x20x20x20) possible forms, because each of the amino acids in the chain could be any one of the 20 that there are available.
The polypeptide chains are some times held in a spiral shape by hydrogen bonds between the amino and carboxylic acid groups. This is called an “Alpha Helix”
ProteinsThis ribbon diagram shows a number of alpha helices
linked together by less structured areas of the polypeptide chain to form the final protein structure
The secondary structures (alpha helices and beta pleated sheets) are held in place by different kinds of bonds , this is the tertiary (third) level of structure
• This means it is made up of more than one polypeptide chain (it does not mean that all quaternary proteins have 4 polypeptide components!)
• The polypeptide chains are held together by similar bonds as the tertiary structure
• The haem area is called a “prosthetic” group. A molecule of oxygen can bind to each haem group
Proteins
Collagen molecules are made of repeating sequences of amino acids that form spiral structures. (Far left picture) Collagen protein is made of 3 polypeptide chains wound together rather like a rope. Hydrogen bonds hold the chains together(second picture from left)Each group of 3 chains is bonded to another group by co-valent bonds called cross links, thus fibrils are formedMany fibrils form a collagen fibreCollagen is a STRUCTURAL protein rather than a globular or metabolic protein