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.


2a50

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2a50.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2a50.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2a50| PDB=2a50 | SCENE= }}
{{STRUCTURE_2a50| PDB=2a50 | SCENE= }}
-
'''fluorescent protein asFP595, wt, off-state'''
+
===fluorescent protein asFP595, wt, off-state===
-
==Overview==
+
<!--
-
Proteins that can be reversibly photoswitched between a fluorescent and a nonfluorescent state bear enormous potential in diverse fields, such as data storage, in vivo protein tracking, and subdiffraction resolution light microscopy. However, these proteins could hitherto not live up to their full potential because the molecular switching mechanism is not resolved. Here, we clarify the molecular photoswitching mechanism of asFP595, a green fluorescent protein (GFP)-like protein that can be transferred from a nonfluorescent "off" to a fluorescent "on" state and back again, by green and blue light, respectively. To this end, we establish reversible photoswitching of fluorescence in whole protein crystals and show that the switching kinetics in the crystal is identical with that in solution. Subsequent x-ray analysis demonstrated that upon the absorption of a green photon, the chromophore isomerizes from a trans (off) to a cis (on) state. Molecular dynamics calculations suggest that isomerization occurs through a bottom hula twist mechanism with concomitant rotation of both bonds of the chromophoric methine ring bridge. This insight into the switching mechanism should facilitate the targeted design of photoswitchable proteins. Reversible photoswitching of the protein chromophore system within intact crystals also constitutes a step toward the use of fluorescent proteins in three-dimensional data recording.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16135569}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16135569 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16135569}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Photochromic protein]]
[[Category: Photochromic protein]]
[[Category: Reversible photoswitch]]
[[Category: Reversible photoswitch]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:36:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:21:21 2008''

Revision as of 03:21, 29 July 2008

Image:2a50.png

Template:STRUCTURE 2a50

fluorescent protein asFP595, wt, off-state

Template:ABSTRACT PUBMED 16135569

About this Structure

2A50 is a Protein complex structure of sequences from Anemonia sulcata. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of the reversible photoswitch of a fluorescent protein., Andresen M, Wahl MC, Stiel AC, Grater F, Schafer LV, Trowitzsch S, Weber G, Eggeling C, Grubmuller H, Hell SW, Jakobs S, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13070-4. Epub 2005 Aug 31. PMID:16135569

Page seeded by OCA on Tue Jul 29 06:21:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a50"
Personal tools