Quaternary Structure: Difference between revisions
Jump to navigation
Jump to search
Cleaned up the entry. Added in some links. Sorted out the references. Poorly formated. Didn't follow publication guidelines. |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
[[Proteins|Proteins]] have a variety of shapes and formations. Proteins can have a quaternary structure; this is the final assembly in which proteins can take. It is when at least 2 or more subunits of [[Polypeptide|polypeptide chains]] interact with each other by forming a range of bonds such as [[ | [[Proteins|Proteins]] have a variety of shapes and formations. Proteins can have a quaternary structure; this is the final assembly in which proteins can take. It is when at least 2 or more subunits of [[Polypeptide|polypeptide chains]] interact with each other by forming a range of bonds such as [[Hydrogen bond|hydrogen bond]], [[Disulphide bridges|disulphide bridges/bonds]] and many more. Each polypeptide chain can vary in their genes they were coded from. An example of a quaternary structure protein is [[Haemoglobin|haemoglobin]]<ref>Millar, T (2006). Biochemistry explained. New York: Taylor and Francis. 51.</ref><ref>Millar, T (2006). Biochemistry explained. New York: Taylor and Francis. 51.</ref><br> | ||
=== References === | === References === | ||
<references / | <references /> | ||
Latest revision as of 01:45, 24 October 2014
Proteins have a variety of shapes and formations. Proteins can have a quaternary structure; this is the final assembly in which proteins can take. It is when at least 2 or more subunits of polypeptide chains interact with each other by forming a range of bonds such as hydrogen bond, disulphide bridges/bonds and many more. Each polypeptide chain can vary in their genes they were coded from. An example of a quaternary structure protein is haemoglobin[1][2]