Tertiary Structure
Tertiary structure
The shape of the tertiary structure is three dimensional due to the coils and pleats folding in on themselves when the protein is formed. The tertiary structure is held in place by lots of different types of bonds. A protein’s tertiary structure is vital to its function; one example would be when a hormone must fit a special type of hormone receptor of a target cell. When you heat a protein, the kinetic energy increase in the molecule. This causes the molecule to vibrate and breaks some of the bonds holding the tertiary structure in place as most of the bonds holding the tertiary structure in place are quite weak, they are easily broken. If enough heat is applied, the whole tertiary structure can unravel and the proteins will no longer function. This process is called denaturation. The protein is said to be denatured. Even if the protein is then cooled, it will return to the orignal shape.
Quaternary structure
Quaternary structure refers to the fact that some proteins are made up of more than one polypeptide subunit joined together. Such proteins only function if all the subunits are present. Quaternary structure may involve two identical polypeptides coming together to form the final working protein, or it may involve a number of different …show more content…
Two are alpha-chains; the other two are beta-chains. The four subunits together form one haemoglobin molecule, which is a water- soluble globular protein. As with all proteins, the tertiary structure of each subunit is held in place by a number bonds and interactions a very specific shape. The shape is vital for the molecule to carry out its function. This shape is vital for the molecule to carry out its function. The haemoglobin's function is to carry oxygen from the lungs to the tissues. It binds in the lungs and release it in the tissues. A specialised part of each polypeptide , called a heam group, contains an iron
The shape of the tertiary structure is three dimensional due to the coils and pleats folding in on themselves when the protein is formed. The tertiary structure is held in place by lots of different types of bonds. A protein’s tertiary structure is vital to its function; one example would be when a hormone must fit a special type of hormone receptor of a target cell. When you heat a protein, the kinetic energy increase in the molecule. This causes the molecule to vibrate and breaks some of the bonds holding the tertiary structure in place as most of the bonds holding the tertiary structure in place are quite weak, they are easily broken. If enough heat is applied, the whole tertiary structure can unravel and the proteins will no longer function. This process is called denaturation. The protein is said to be denatured. Even if the protein is then cooled, it will return to the orignal shape.
Quaternary structure
Quaternary structure refers to the fact that some proteins are made up of more than one polypeptide subunit joined together. Such proteins only function if all the subunits are present. Quaternary structure may involve two identical polypeptides coming together to form the final working protein, or it may involve a number of different …show more content…
Two are alpha-chains; the other two are beta-chains. The four subunits together form one haemoglobin molecule, which is a water- soluble globular protein. As with all proteins, the tertiary structure of each subunit is held in place by a number bonds and interactions a very specific shape. The shape is vital for the molecule to carry out its function. This shape is vital for the molecule to carry out its function. The haemoglobin's function is to carry oxygen from the lungs to the tissues. It binds in the lungs and release it in the tissues. A specialised part of each polypeptide , called a heam group, contains an iron