1bx3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bx3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1bx3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bx3| PDB=1bx3 | SCENE= }}
{{STRUCTURE_1bx3| PDB=1bx3 | SCENE= }}
-
'''EFFECTS OF COMMONLY USED CRYOPROTECTANTS ON GLYCOGEN PHOSPHORYLASE ACTIVITY AND STRUCTURE'''
+
===EFFECTS OF COMMONLY USED CRYOPROTECTANTS ON GLYCOGEN PHOSPHORYLASE ACTIVITY AND STRUCTURE===
-
==Overview==
+
<!--
-
The effects of a number of cryoprotectants on the kinetic and structural properties of glycogen phosphorylase b have been investigated. Kinetic studies showed that glycerol, one of the most commonly used cryoprotectants in X-ray crystallographic studies, is a competitive inhibitor with respect to substrate glucose-1-P with an apparent Ki value of 3.8% (v/v). Cryogenic experiments, with the enzyme, have shown that glycerol binds at the catalytic site and competes with glucose analogues that bind at the catalytic site, thus preventing the formation of complexes. This necessitated a change in the conditions for cryoprotection in crystallographic binding experiments with glycogen phosphorylase. It was found that 2-methyl-2,4-pentanediol (MPD), polyethylene glycols (PEGs) of various molecular weights, and dimethyl sulfoxide (DMSO) activated glycogen phosphorylase b to different extents, by stabilizing its most active conformation, while sucrose acted as a noncompetitive inhibitor and ethylene glycol as an uncompetitive inhibitor with respect to glucose-1-P. A parallel experimental investigation by X-ray crystallography showed that, at 100 K, both MPD and DMSO do not bind at the catalytic site, do not induce any significant conformational change on the enzyme molecule, and hence, are more suitable cryoprotectants than glycerol for binding studies with glycogen phosphorylase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10211820}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10211820 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10211820}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Mpd]]
[[Category: Mpd]]
[[Category: Phosphorylase]]
[[Category: Phosphorylase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:03:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:51:14 2008''

Revision as of 16:51, 30 June 2008

Template:STRUCTURE 1bx3

EFFECTS OF COMMONLY USED CRYOPROTECTANTS ON GLYCOGEN PHOSPHORYLASE ACTIVITY AND STRUCTURE

Template:ABSTRACT PUBMED 10211820

About this Structure

1BX3 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure., Tsitsanou KE, Oikonomakos NG, Zographos SE, Skamnaki VT, Gregoriou M, Watson KA, Johnson LN, Fleet GW, Protein Sci. 1999 Apr;8(4):741-9. PMID:10211820

Page seeded by OCA on Mon Jun 30 19:51:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools