Globular proteins: Difference between revisions
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Globular | Globular proteins are spherical in shape and usually water soluble. Examples of globular proteins include [[Haemoglobin|haemoglobin]], [[Insulin|insulin]] and many [[Enzymes|enzymes]] in the body. The increased solubility of the [[Proteins|proteins]] is all down to the folding of the protein<ref>http://elmhurst.edu/~chm/vchembook/568globularprotein.html</ref>. The protein folds in such a way that places the [[Hydrophobic|hydrophobic]] parts of the chain on the inside and the [[Hydrophilic|hydrophilic]] parts on the outside of the chain. This allows for the hydrophilic sections to form intermolecular forces with water [[Molecules|molecules]] dissolving the protein. The hydrophilic part of the protein contains [[Amino acids|amino acids]] with [[Polar side chains|polar side chains]]. These will have the opposite charge to either the [[Hydrogen|hydrogen’s]] or [[Oxygen|oxygen]] in [[Water|water]], allowing forces to be set up between the protein and water. Many water molecules will associate with a single protein as they are large structures compared to water<ref>http://www.chemistryexplained.com/Ge-Hy/Globular-Protein.html</ref>. The structure of the globular protein is relatively stable because of the non-covalent interactions such as the hydrophobic interactions which stabilize the structure in a margin. These proteins are quite sensitive to pH, temperature and other factors as well<ref>http://ib.bioninja.com.au/standard-level/topic-2-molecular-biology/24-proteins/fibrous-vs-globular-protein.html</ref>. | ||
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Latest revision as of 12:36, 4 December 2017
Globular proteins are spherical in shape and usually water soluble. Examples of globular proteins include haemoglobin, insulin and many enzymes in the body. The increased solubility of the proteins is all down to the folding of the protein[1]. The protein folds in such a way that places the hydrophobic parts of the chain on the inside and the hydrophilic parts on the outside of the chain. This allows for the hydrophilic sections to form intermolecular forces with water molecules dissolving the protein. The hydrophilic part of the protein contains amino acids with polar side chains. These will have the opposite charge to either the hydrogen’s or oxygen in water, allowing forces to be set up between the protein and water. Many water molecules will associate with a single protein as they are large structures compared to water[2]. The structure of the globular protein is relatively stable because of the non-covalent interactions such as the hydrophobic interactions which stabilize the structure in a margin. These proteins are quite sensitive to pH, temperature and other factors as well[3].