Sandbox Reserved 196: Difference between revisions
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{{Template:Johnson_CH462_Spring2011}} | {{Template:Johnson_CH462_Spring2011}} | ||
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Ribonuclease 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. | Ribonuclease 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. | ||
== Background == | == Background == | ||
2D pic (left) | 2D pic (left) | ||
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3D pic (Right) | 3D pic (Right) | ||
have at least 2 green links | have at least 2 green links | ||
<Structure load='1rbb' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_196/Rbb_basic/1' /> | |||
== Biology of RNase B == | == Biology of RNase B == | ||
