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Sandbox Reserved 196

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Revision as of 15:18, 29 March 2011 by Carissa Fuller (Talk | contribs)
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This Sandbox is Reserved from Feb 02, 2011, through Jul 31, 2011 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 191 through Sandbox Reserved 200.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert a 3D applet Jmol scene window.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


Contents

Introduction

RNase B is a glycoprotein that can that cleave N-linked carbohydrates (1). RNase B is structurally the same as RNase A. However is has an additional catalytic activity caused by the attachment of polysaccharrides at the Asn-34. This small change allows RNase B to hydrolyze double-stranded RNA at ionic strengths where RNase A has no activity. This shows that small changes in the active sites of very similar molecules can lead to todally new roles and activities. (2)

Background

Image:RNaseB.png
RNase B

3D pic (Right) have at least 2 green links

3D picture of RNase B dimer

Drag the structure with the mouse to rotate

Ribonuclease B with a strand of DNA in active site

Drag the structure with the mouse to rotate


Biology of RNase B

green links

Description

References

[1]
  1. ↑ New England Bio Lab, INC http://www.neb.com/nebecomm/products/productP7817.asp
[1]
  1. ↑ Williams RL, Greene SM, McPherson A. The crystal structure of ribonuclease B at 2.5-A resolution. J Biol Chem. 1987 Nov 25;262(33):16020-31. PMID:3680242


Additional Resources

  • Dr. Johnson
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