Globular proteins: Difference between revisions

From The School of Biomedical Sciences Wiki
Jump to navigation Jump to search
No edit summary
Nnjm2 (talk | contribs)
Not one link! Not correctly referenced...
Line 1: Line 1:
Globular proteins&nbsp;are spherical in shape and usually water soluble. They 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]<br>References: <br>1. http://elmhurst.edu/~chm/vchembook/568globularprotein.html<br>2. http://www.chemistryexplained.com/Ge-Hy/Globular-Protein.html <br><br>
Globular proteins&nbsp;are spherical in shape and usually water soluble. They 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>.&nbsp;&nbsp;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&nbsp;<ref>http://www.chemistryexplained.com/Ge-Hy/Globular-Protein.html</ref>
 
=== References  ===
 
<references /><br><br>

Revision as of 09:44, 28 November 2014

Globular proteins are spherical in shape and usually water soluble. They 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]

References