1ouu: Difference between revisions

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==Overview==

We have determined the X-ray crystallographic structure of trout Hb I in, both the deoxy and carbonmonoxy forms to resolution limits of 2.3, angstroms and 2.5 angstroms, respectively. The overall fold of the, molecule is highly similar to that of human HbA despite the low level of, sequence identity between these proteins. Trout Hb I is unusual in, displaying almost no pH dependence of oxygen binding affinity, and (at, most) very weak interactions with heterotropic effector ligands such as, organic phosphates. Comparison of the two quaternary states of the protein, indicates how such effects are minimised and how the low-affinity T state, of the protein is stabilised in the absence of heterotropic interactions.

We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions.

==About this Structure==

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[[Category: respiratory protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:36:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:48 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-We have determined the X-ray crystallographic structure of trout Hb I in, both the deoxy and carbonmonoxy forms to resolution limits of 2.3, angstroms and 2.5 angstroms, respectively. The overall fold of the, molecule is highly similar to that of human HbA despite the low level of, sequence identity between these proteins. Trout Hb I is unusual in, displaying almost no pH dependence of oxygen binding affinity, and (at, most) very weak interactions with heterotropic effector ligands such as, organic phosphates. Comparison of the two quaternary states of the protein, indicates how such effects are minimised and how the low-affinity T state, of the protein is stabilised in the absence of heterotropic interactions.
+We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions.
 ==About this Structure==
@@ Line 23: / Line 23: @@
 [[Category: respiratory protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:36:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:48 2008''