2bwh
From Proteopedia
| Line 28: | Line 28: | ||
[[Category: time-resolved x-ray structure determination]] | [[Category: time-resolved x-ray structure determination]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:50:03 2007'' |
Revision as of 14:45, 30 October 2007
|
LAUE STRUCTURE OF A SHORT LIVED STATE OF L29W MYOGLOBIN
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 ... [(full description)]
About this Structure
2BWH is a [Single protein] structure of sequence from [[1]] with HEM and CMO as [ligands]. Structure known Active Site: AC1. 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 Oct 30 16:50:03 2007
