1ajg: Difference between revisions

Line 1:

[[Image:1ajg.~~gif~~|left|200px]]

[[Image:1ajg.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~CARBONMONOXY MYOGLOBIN AT 40 K~~'''~~

===CARBONMONOXY MYOGLOBIN AT 40 K===

~~==Overview==~~

<!--

Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ~~ns time scales for these processes are still much shorter than~~ the ~~ms time resolution of X-ray diffraction experiments, but~~ it ~~may be possible to trap these intermediates~~ at ~~low temperatures~~. ~~We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K~~. ~~Our results provide a structural basis for~~ the ~~interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins~~.

The line below this paragraph, {{ABSTRACT_PUBMED_7634074}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7634074 is the PubMed ID number.

-->

==About this Structure==

Line 28:

Line 32:

[[Category: Oxygen transport]]

[[Category: Respiratory protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:21:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:58:49 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1ajg.gif|left|200px]]
+{{Seed}}
+[[Image:1ajg.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ajg|  PDB=1ajg  |  SCENE=  }}
-'''CARBONMONOXY MYOGLOBIN AT 40 K'''
+===CARBONMONOXY MYOGLOBIN AT 40 K===
-==Overview==
+<!--
-Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_7634074}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7634074 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7634074}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Oxygen transport]]
 [[Category: Respiratory protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:21:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:58:49 2008''