Sandbox Reserved 196: Difference between revisions

Line 11:

== Structure and Biology of RNase B ==

[[Image:RNaseB.png | thumb|left|RNase B]]

RNase A and RNase B have identical primary structures; however, RNase B is bound to mannose carbohydrates. This glycosylation increases the <Structure load='1rbj' size='250' frame='true' align='right' caption='Ribonuclease B with a strand of DNA in active site' scene='Sandbox_Reserved_196/Secondary_structure/8' name ='1rbj' />~~kinetic stability of RNase B by 3 kj/mol compared to RNase A <ref name="third">PMID:10600722</ref>. Gycosylated, RNase B however, is not significantly different by NMR in protein~~ conformation to RNase A <ref name="fourth">PMID:1322837</ref>.

RNase A and RNase B have identical primary structures; however, RNase B is bound to mannose carbohydrates. This glycosylation increases the kinetic stability of RNase B by 3 kj/mol compared to RNase A <ref name="third">PMID:10600722</ref>. Gycosylated, RNase B however, is not significantly different by NMR in protein <Structure load='1rbj' size='250' frame='true' align='right' caption='Ribonuclease B with a strand of DNA in active site' scene='Sandbox_Reserved_196/Secondary_structure/8' name ='1rbj' />conformation to RNase A <ref name="fourth">PMID:1322837</ref>.

Slight differences indclude changes in crystal packing. RNase B crystals have two slightly asymmetrical units. The crystals are dimeric with two separate molecules, I and II, which are linked by a salt bridge at Asp-121 and Arg-85. This linkage determines the orientation of the two molecules in relation to one another. Not only does a salt bridge link this dimer-type molecule, but other ions also interact via cross-linkage to stabilize the structure <ref name="second" />.

Sandbox Reserved 196: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 11: / Line 11: @@
 == Structure and Biology of RNase B ==
 [[Image:RNaseB.png | thumb|left|RNase B]]
-RNase A and RNase B have identical primary structures; however, RNase B is bound to mannose carbohydrates. This glycosylation increases the <Structure load='1rbj' size='250' frame='true' align='right' caption='Ribonuclease B with a strand of DNA in active site' scene='Sandbox_Reserved_196/Secondary_structure/8' name ='1rbj' />kinetic stability of RNase B by 3 kj/mol compared to RNase A <ref name="third">PMID:10600722</ref>. Gycosylated, RNase B however, is not significantly different by NMR in protein conformation to RNase A <ref name="fourth">PMID:1322837</ref>.
+RNase A and RNase B have identical primary structures; however, RNase B is bound to mannose carbohydrates. This glycosylation increases the kinetic stability of RNase B by 3 kj/mol compared to RNase A <ref name="third">PMID:10600722</ref>. Gycosylated, RNase B however, is not significantly different by NMR in protein <Structure load='1rbj' size='250' frame='true' align='right' caption='Ribonuclease B with a strand of DNA in active site' scene='Sandbox_Reserved_196/Secondary_structure/8' name ='1rbj' />conformation to RNase A <ref name="fourth">PMID:1322837</ref>.
 Slight differences indclude changes in crystal packing. RNase B crystals have two slightly asymmetrical units. The crystals are dimeric with two separate molecules, I and II, which are linked by a salt bridge at Asp-121 and Arg-85. This linkage determines the orientation of the two molecules in relation to one another. Not only does a salt bridge link this dimer-type molecule, but other ions also interact via cross-linkage to stabilize the structure <ref name="second" />.