Sandbox 42: Difference between revisions
From Proteopedia
Jump to navigationJump to search
mNo edit summary |
mNo edit summary |
||
| Line 7: | Line 7: | ||
The primary catalytic action of the enzyme lysozyme is to hydrolyze β(1→4) glycosidic linkages found in bacterial cell walls.<ref>http://lysozyme.co.uk/</ref> More specifically, lysozyme hydrolyzes the linkages from ''N''-acetylmuramic acid to ''N''-acetylglucosamine which occur in peptidoglycans of the cell wall. The small 14.3 kD Hen egg white lysozyme is one of the most widely studied lysozymes. | The primary catalytic action of the enzyme lysozyme is to hydrolyze β(1→4) glycosidic linkages found in bacterial cell walls.<ref>http://lysozyme.co.uk/</ref> More specifically, lysozyme hydrolyzes the linkages from ''N''-acetylmuramic acid to ''N''-acetylglucosamine which occur in peptidoglycans of the cell wall. The small 14.3 kD Hen egg white lysozyme is one of the most widely studied lysozymes. | ||
== Secondary structure == | == Secondary structure == | ||
Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. 4 disulfide bonds are involved in folding of the chain. | Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. Important<scene name='Sandbox_42/Seconday_Structure/1'>secondary structures</scene> formed by the chain include 7 alpha helicies and 1 beta sheet consisting of 3 anti-parallel strands. 4 disulfide bonds are involved in folding of the chain. | ||
== Distribution of residue polarity == | == Distribution of residue polarity == | ||
