Sandbox 31: Difference between revisions

Line 23:

Papain is formed from a peptide that is 212 amino acids in length. It consists of 25% <scene name='Sandbox_31/Alpha_helices/4'>Alpha helices</scene> and 21% <scene name='Sandbox_31/Beta_sheet/2'>Beta Sheet</scene>. The structure also consists of three <scene name='Sandbox_31/Disulfide/3'>Disulfide bonds</scene> between <scene name='Sandbox_31/Cys_with_labels/2'>Cysteine Residues</scene>. The disulfide bonds exist between Cys 63 and Cys 22, Cys 200 and Cys 153, and Cys 56 and Cys 95. Another important residue to the structure is Cysteine 25 which has a sulfhydryl group that plays a major role in the active site activity[[http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html]].

The <scene name='Sandbox_31/Hydrophobic_residues/2'>Hydrophobic Residues</scene> in papain are primarily located toward the inside of the enzyme or paired by hydrophobic interactions with other hydrophobic residues to exclude water. The <scene name='Sandbox_31/Charged/2'>Polar Residues</scene> are located facing the exterior, in the active site, or paired with other charged residues. The charged and polar residues are hydrophilic therefore do not orient themselves to exclude water or solvent. The charged <scene name='Sandbox_31/Termini/4'>Termini</scene> face outward due to their hydrophilic nature.

The <scene name='Sandbox_31/Hydrophobic_residues/2'>Hydrophobic Residues</scene> in papain are primarily located toward the inside of the enzyme or paired by hydrophobic interactions with other hydrophobic residues to exclude water. The <scene name='Sandbox_31/Charged/2'>Polar Residues</scene> are located facing the exterior, in the active site, or paired with other charged residues. The <scene name='Sandbox_31/Positive/1'>Negatively</scene> charged residues (acidic) and the <scene name='Sandbox_31/Basic_positive/1'>Negatively</scene> charged residues (basic) make up the polar residues. The charged and polar residues are hydrophilic therefore do not orient themselves to exclude water or solvent. The charged <scene name='Sandbox_31/Termini/4'>Termini</scene> face outward due to their hydrophilic nature.

Sandbox 31: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 17:36, 14 November 2011 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 17:53, 14 November 2011 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
Line 23:		Line 23:
	Papain is formed from a peptide that is 212 amino acids in length. It consists of 25% <scene name='Sandbox_31/Alpha_helices/4'>Alpha helices</scene> and 21% <scene name='Sandbox_31/Beta_sheet/2'>Beta Sheet</scene>. The structure also consists of three <scene name='Sandbox_31/Disulfide/3'>Disulfide bonds</scene> between <scene name='Sandbox_31/Cys_with_labels/2'>Cysteine Residues</scene>. The disulfide bonds exist between Cys 63 and Cys 22, Cys 200 and Cys 153, and Cys 56 and Cys 95. Another important residue to the structure is Cysteine 25 which has a sulfhydryl group that plays a major role in the active site activity[[http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html]].		Papain is formed from a peptide that is 212 amino acids in length. It consists of 25% <scene name='Sandbox_31/Alpha_helices/4'>Alpha helices</scene> and 21% <scene name='Sandbox_31/Beta_sheet/2'>Beta Sheet</scene>. The structure also consists of three <scene name='Sandbox_31/Disulfide/3'>Disulfide bonds</scene> between <scene name='Sandbox_31/Cys_with_labels/2'>Cysteine Residues</scene>. The disulfide bonds exist between Cys 63 and Cys 22, Cys 200 and Cys 153, and Cys 56 and Cys 95. Another important residue to the structure is Cysteine 25 which has a sulfhydryl group that plays a major role in the active site activity[[http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html]].

	The <scene name='Sandbox_31/Hydrophobic_residues/2'>Hydrophobic Residues</scene> in papain are primarily located toward the inside of the enzyme or paired by hydrophobic interactions with other hydrophobic residues to exclude water. The <scene name='Sandbox_31/Charged/2'>Polar Residues</scene> are located facing the exterior, in the active site, or paired with other charged residues. The charged and polar residues are hydrophilic therefore do not orient themselves to exclude water or solvent. The charged <scene name='Sandbox_31/Termini/4'>Termini</scene> face outward due to their hydrophilic nature.		The <scene name='Sandbox_31/Hydrophobic_residues/2'>Hydrophobic Residues</scene> in papain are primarily located toward the inside of the enzyme or paired by hydrophobic interactions with other hydrophobic residues to exclude water. The <scene name='Sandbox_31/Charged/2'>Polar Residues</scene> are located facing the exterior, in the active site, or paired with other charged residues. The <scene name='Sandbox_31/Positive/1'>Negatively</scene> charged residues (acidic) and the <scene name='Sandbox_31/Basic_positive/1'>Negatively</scene> charged residues (basic) make up the polar residues. The charged and polar residues are hydrophilic therefore do not orient themselves to exclude water or solvent. The charged <scene name='Sandbox_31/Termini/4'>Termini</scene> face outward due to their hydrophilic nature.