Sandbox Reserved 196: Difference between revisions

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== Introduction ==
== 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)
RNase B is a glycoprotein that can that cleave N-linked carbohydrates <ref>New England Bio Lab, INC http://www.neb.com/nebecomm/products/productP7817.asp</ref>. 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. <ref>PMID:3680242</ref>
== Background ==
== Background ==
[[Image:RNaseB.png | thumb|left|RNase B]]
[[Image:RNaseB.png | thumb|left|RNase B]]
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== References ==
== References ==
<ref group=>New England Bio Lab, INC http://www.neb.com/nebecomm/products/productP7817.asp</ref><references />
<ref group=>PMID:3680242</ref><references />


== Additional Resources ==
== Additional Resources ==
<ref group="xtra">Dr. Johnson</ref>
<ref group="xtra">Dr. Johnson</ref>
<references group="xtra"/>
<references group="xtra"/>

Revision as of 15:27, 29 March 2011

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.
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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

File:RNaseB.png
RNase B

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

3D picture of RNase B dimer

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Ribonuclease B with a strand of DNA in active site

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Biology of RNase B

green links

Description

References

Additional Resources

  1. Dr. Johnson
  1. ↑ New England Bio Lab, INC https://www.neb.com/nebecomm/products/productP7817.asp
  2. ↑ 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
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