This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Sandbox 45

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:21, 16 October 2012) (edit) (undo)
 
(199 intermediate revisions not shown.)
Line 1: Line 1:
 +
<!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
 +
{{Template:Oberholser_Sandbox_Reservation}}
 +
<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
 +
==Introduction==
 +
<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here' />
 +
<scene name='Sandbox_45/Ak_backbone/1'>Backbone</scene>
 +
<scene name='Sandbox_45/Ak_alpha_helix_2/1'>Alpha Helices</scene>
 +
<scene name='Sandbox_45/Ak_beta_sheet/1'>Beta Sheet</scene>
 +
<scene name='Sandbox_45/Ak_alpha_beta_sheet/1'>secondary structure</scene>
 +
<scene name='Sandbox_45/Ak_hbonds/1'>Hydrogen Bonds</scene>
 +
<scene name='Sandbox_45/Ak_hydrophobic_residues/1'>Hydrophobic residues</scene>
 +
<scene name='Sandbox_45/Ak_hydrophilic_residues/1'>Hydrophilic residues</scene>
-
= Structure of Trypsin =
+
<scene name='Sandbox_45/Ak_hbonds_actual/1'>The Hydrogen Bonds</scene>
-
----
+
-
 
+
-
 
+
-
 
+
-
== Primary ==
+
-
Bovine trypsin contains 223 amino acid residues of varied interactive tendencies and chemical characteristics, each of which contribute to the protein's structure and catalytic function.
+
-
== Secondary ==
+
-
The spacial arrangement of hydrophobic and hydrophilic residues
+
-
 
+
-
<scene name='Sandbox_45/Bt-helix/1'>alpha helices</scene>
+
-
 
+
-
<scene name='Sandbox_45/Bt-sheet1/1'>beta sheets</scene>
+
-
[[Image:Topographytrypsin.gif|thumb|center|upright=2.0]]
+
-
 
+
-
 
+
-
sig of disulfides in overall structure, helix to beta sheet,
+
-
 
+
-
<scene name='Sandbox_45/Helixhold_hbond/1'>hydrogen bonding and water bridges</scene>
+
-
 
+
-
<scene name='Sandbox_45/Helixhold_vanderwaals/1'>van der Waals forces</scene>
+
-
<applet load='3LJJ' size='300' frame='true' align='right' caption='Bovine Trypsin' />
+
-
 
+
-
<scene name='Sandbox_45/Bt-phillic/1'>hydrophilic residues</scene>
+
-
 
+
-
<scene name='Sandbox_45/Bt-phillic/3'>hydrophobic residues</scene>
+
-
 
+
-
<scene name='Sandbox_45/Bt-phillic_waters/2'>water interaction</scene>
+
-
 
+
-
<scene name='Sandbox_45/Bt-phillic_waters/3'>transparent</scene>
+
-
 
+
-
== Ligand Binding and Catalysis ==
+
-
 
+
-
<scene name='Sandbox_45/Btligand/1'>ligands</scene>
+
-
 
+
-
<scene name='Sandbox_45/Btsulfates/1'>sulfate ions</scene>
+
-
 
+
-
key amino acids
+
-
 
+
-
<scene name='Sandbox_45/Lig-metal/1'>metal</scene>
+
-
 
+
-
<scene name='Sandbox_45/Lig-waterbridge/1'>water bridges</scene>
+
-
 
+
-
<scene name='Sandbox_45/Lig-hydrogenbond/1'>hydrogen bonds</scene>
+
-
 
+
-
<scene name='Sandbox_45/Specificity_pocket/1'>specificity pocket</scene>
+
-
 
+
-
[[Image:Ligandinteractionstrypsin.gif|thumb|center|upright=2.0]]
+
-
 
+
-
<scene name='Sandbox_45/Catalytic_triad/1'>catalytic triad</scene>
+

Current revision

Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.

Introduction

Adenylate Kinase

Drag the structure with the mouse to rotate

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_45"
Personal tools