1mgn: Difference between revisions

Revision as of 23:54, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mgn.png

Template:STRUCTURE 1mgn

HIS64(E7)-> TYR APOMYOGLOBIN AS A REAGENT FOR MEASURING RATES OF HEMIN DISSOCIATIONHIS64(E7)-> TYR APOMYOGLOBIN AS A REAGENT FOR MEASURING RATES OF HEMIN DISSOCIATION

Template:ABSTRACT PUBMED 8307983

About this StructureAbout this Structure

1MGN is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

ReferenceReference

His64(E7)-->Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation., Hargrove MS, Singleton EW, Quillin ML, Ortiz LA, Phillips GN Jr, Olson JS, Mathews AJ, J Biol Chem. 1994 Feb 11;269(6):4207-14. PMID:8307983

Page seeded by OCA on Wed Jul 2 23:54:55 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1mgn.gif|left|200px]]
+{{Seed}}
+[[Image:1mgn.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1mgn|  PDB=1mgn  |  SCENE=  }}
-'''HIS64(E7)-> TYR APOMYOGLOBIN AS A REAGENT FOR MEASURING RATES OF HEMIN DISSOCIATION'''
+===HIS64(E7)-> TYR APOMYOGLOBIN AS A REAGENT FOR MEASURING RATES OF HEMIN DISSOCIATION===
-==Overview==
+<!--
-To develop an assay for hemin dissociation, His64(E7) was replaced by Tyr in sperm whale myoglobin producing a holoprotein with a distinct green color due to an intense absorption band at 600 nm. Val68(E11) was replaced by Phe in the same protein to increase its stability. When excess Tyr64-Val68 apoglobin is mixed with either metmyoglobin or methemoglobin, the solution turns from brown to green, and the absorbance changes can be used to measure complete time courses for hemin dissociation from either holoprotein. This assay has been used to measure rates of hemin dissociation from native metmyoglobin, four myoglobin mutants (Ala64(E7), Ala68(E11), Phe68(E11), and Glu45(CD3)), native methemoglobin, valence hybrid hemoglobins, and two mutant hemoglobins ((alpha(Gly-E7)beta(native))2, and (alpha(native)beta(Gly-E7))2). Two kinetic phases were observed for hemin dissociation from native human hemoglobin at pH 7.0 and 37 degrees C. Valence and mutant hybrid hemoglobins were used to assign the faster phase (k = 7.8 +/- 2.0 h-1) to hemin dissociation from ferric beta subunits and the slower (k = 0.6 +/- 0.15 h-1) to dissociation from alpha subunits. The corresponding rate for wild-type metmyoglobin is 0.007 +/- 0.004 h-1.
+The line below this paragraph, {{ABSTRACT_PUBMED_8307983}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8307983 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8307983}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Quillin, M L.]]
 [[Category: Oxygen transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:59:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 23:54:55 2008''