Proteins: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
Proteins are polymer structures made from different [[ | Proteins are polymer structures made from different [[Amino acids|amino acids]]. The number of [[Amino_acids|amino acids]] within a sequence can vary from 20 [[Amino acids|amino acids]] to thousands of [[Amino_acids|amino acids]] long. | ||
There are 4 different structures that proteins can have: | There are 4 different structures that proteins can have: | ||
1.[[Primary Protein Structure|Primary Structure ]]- linear amino acid sequence <br>2.[[Secondary Protein Structure|Secondary Structure ]]- gives rise to an alpha helix or beta pleated sheet held together by hydrogen bonds. | 1. [[Primary Protein Structure|Primary Structure ]]- linear amino acid sequence <br>2. [[Secondary Protein Structure|Secondary Structure ]]- gives rise to an alpha helix or beta pleated sheet held together by hydrogen bonds <ref>Elliott.W.H, Elliott.D.C (1997) Biochemistry and Molecular Biology. New York, United States:Oxford University Press.pp.47-49.ISBN 0199271992</ref>.<br>3. [[Tertiary Protein Structure|Tertiary Structure ]]- gives rise to a single peptide 3D structure held together by various bonds such as [[Hydrogen bonds|hydrogen bonding]], [[Disulphide bonds|disulphide bonding]], salt bridges and non-polar hydrophobic interactions.<br>4. [[Quaternary Protein Structure|Quaternary Structure]] - describes multiple peptide chains that interact through various types of bonding to form a fully functional protein e.g. haemoglobin. | ||
=== References === | |||
<references /> | |||
Revision as of 18:11, 15 November 2010
Proteins are polymer structures made from different amino acids. The number of amino acids within a sequence can vary from 20 amino acids to thousands of amino acids long.
There are 4 different structures that proteins can have:
1. Primary Structure - linear amino acid sequence
2. Secondary Structure - gives rise to an alpha helix or beta pleated sheet held together by hydrogen bonds [1].
3. Tertiary Structure - gives rise to a single peptide 3D structure held together by various bonds such as hydrogen bonding, disulphide bonding, salt bridges and non-polar hydrophobic interactions.
4. Quaternary Structure - describes multiple peptide chains that interact through various types of bonding to form a fully functional protein e.g. haemoglobin.
References
- ↑ Elliott.W.H, Elliott.D.C (1997) Biochemistry and Molecular Biology. New York, United States:Oxford University Press.pp.47-49.ISBN 0199271992