1jp9: Difference between revisions

Revision as of 14:25, 21 February 2008

Sperm Whale met-Myoglobin (low temperature; high pressure)

OverviewOverview

Pressures in the 100 MPa range are known to have an enormous number of effects on the action of proteins, but straightforward means for determining the structural basis of these effects have been lacking. Here, crystallography has been used to probe effects of pressure on sperm whale myoglobin structure. A comparison of pressure effects with those seen at low pH suggests that structural changes under pressure are interpretable as a shift in the populations of conformational substates. Furthermore, a novel high-pressure protein crystal-cooling method has been used to show low-temperature metastability, providing an alternative to room temperature, beryllium pressure cell-based techniques. The change in protein structure due to pressure is not purely compressive and involves conformational changes important to protein activity. Correlation with low-pH structures suggests observed structural changes are associated with global conformational substates. Methods developed here open up a direct avenue for exploration of the effects of pressure on proteins.

About this StructureAbout this Structure

1JP9 is a Single protein structure of sequence from Physeter catodon with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Probing substates in sperm whale myoglobin using high-pressure crystallography., Urayama P, Phillips GN Jr, Gruner SM, Structure. 2002 Jan;10(1):51-60. PMID:11796110

Page seeded by OCA on Thu Feb 21 13:25:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1jp9.jpg|left|200px]]<br /><applet load="1jp9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jp9.jpg|left|200px]]<br /><applet load="1jp9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jp9, resolution 1.70&Aring;" />
 '''Sperm Whale met-Myoglobin (low temperature; high pressure)'''<br />
 ==Overview==
-Pressures in the 100 MPa range are known to have an enormous number of, effects on the action of proteins, but straightforward means for, determining the structural basis of these effects have been lacking. Here, crystallography has been used to probe effects of pressure on sperm whale, myoglobin structure. A comparison of pressure effects with those seen at, low pH suggests that structural changes under pressure are interpretable, as a shift in the populations of conformational substates. Furthermore, a, novel high-pressure protein crystal-cooling method has been used to show, low-temperature metastability, providing an alternative to room, temperature, beryllium pressure cell-based techniques. The change in, protein structure due to pressure is not purely compressive and involves, conformational changes important to protein activity. Correlation with, low-pH structures suggests observed structural changes are associated with, global conformational substates. Methods developed here open up a direct, avenue for exploration of the effects of pressure on proteins.
+Pressures in the 100 MPa range are known to have an enormous number of effects on the action of proteins, but straightforward means for determining the structural basis of these effects have been lacking. Here, crystallography has been used to probe effects of pressure on sperm whale myoglobin structure. A comparison of pressure effects with those seen at low pH suggests that structural changes under pressure are interpretable as a shift in the populations of conformational substates. Furthermore, a novel high-pressure protein crystal-cooling method has been used to show low-temperature metastability, providing an alternative to room temperature, beryllium pressure cell-based techniques. The change in protein structure due to pressure is not purely compressive and involves conformational changes important to protein activity. Correlation with low-pH structures suggests observed structural changes are associated with global conformational substates. Methods developed here open up a direct avenue for exploration of the effects of pressure on proteins.
 ==About this Structure==
-JP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JP9 OCA].
+JP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JP9 OCA].
 ==Reference==
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 [[Category: Physeter catodon]]
 [[Category: Single protein]]
-[[Category: Gruner, S.M.]]
+[[Category: Gruner, S M.]]
-[[Category: Jr., G.N.Phillips.]]
+[[Category: Jr., G N.Phillips.]]
 [[Category: Urayama, P.]]
 [[Category: HEM]]
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 [[Category: oxygen storage/transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:26:51 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:15 2008''