This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2bw9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bw9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bw9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bw9| PDB=2bw9 | SCENE= }}
{{STRUCTURE_2bw9| PDB=2bw9 | SCENE= }}
-
'''LAUE STRUCTURE OF L29W MBCO'''
+
===LAUE STRUCTURE OF L29W MBCO===
-
==Overview==
+
<!--
-
By using time-resolved x-ray crystallography at room temperature, structural relaxations and ligand migration were examined in myoglobin (Mb) mutant L29W from nanoseconds to seconds after photodissociation of carbon monoxide (CO) from the heme iron by nanosecond laser pulses. The data were analyzed in terms of transient kinetics by fitting trial functions to integrated difference electron density values obtained from select structural moieties, thus allowing a quantitative description of the processes involved. The observed relaxations are linked to other investigations on protein dynamics. At the earliest times, the heme has already completely relaxed into its domed deoxy structure, and there is no photo-dissociated CO visible at the primary docking site. Initial relaxations of larger globin moieties are completed within several hundred nanoseconds. They influence the concomitant migration of photo-dissociated CO to the Xe1 site, where it appears at approximately 300 ns and leaves again at approximately 1.5 ms. The extremely long residence time in Xe1 as compared with wild-type MbCO implies that, in the latter protein, the CO exits the protein from Xe1 predominantly via the distal pocket. A well-defined deligated state is populated between approximately 2 micros and approximately 1 ms; its structure is very similar to the equilibrium deoxy structure. Between 1.5 and 20 ms, no CO is visible in the protein interior; it is either distributed among many sites within the protein or has escaped to the solvent. Finally, recombination at the heme iron occurs after &gt;20 ms.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16085709}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16085709 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16085709}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Laue crystallography]]
[[Category: Laue crystallography]]
[[Category: Myoglobin mutant l29w]]
[[Category: Myoglobin mutant l29w]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:53:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:37:19 2008''

Revision as of 05:37, 29 July 2008

Image:2bw9.png

Template:STRUCTURE 2bw9

LAUE STRUCTURE OF L29W MBCO

Template:ABSTRACT PUBMED 16085709

About this Structure

2BW9 is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

Reference

Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO., Schmidt M, Nienhaus K, Pahl R, Krasselt A, Anderson S, Parak F, Nienhaus GU, Srajer V, Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11704-9. Epub 2005 Aug 5. PMID:16085709

Page seeded by OCA on Tue Jul 29 08:37:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bw9"
Personal tools