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.


1xei

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xei.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xei.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xei| PDB=1xei | SCENE= }}
{{STRUCTURE_1xei| PDB=1xei | SCENE= }}
-
'''THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION'''
+
===THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION===
-
==Overview==
+
<!--
-
Earlier studies involving water-mediated transformations in lysozyme and ribonuclease A have shown that the overall movements in the protein molecule consequent to the reduction in the amount of surrounding water are similar to those that occur during enzyme action, thus highlighting the relationship among hydration, plasticity, and action of these enzymes. Monoclinic lysozyme retains its crystallinity even when the level of hydration is reduced further below that necessary for activity (about 0.2 gram of water per gram of protein). In order to gain insights into the role of water in the stability and the plasticity of the protein molecule and the geometrical basis for the loss of activity that accompanies dehydration, the crystal structures of monoclinic lysozyme with solvent contents of 17.6%, 16.9%, and 9.4% were determined and refined. A detailed comparison of these forms with the normally hydrated forms show that the C-terminal segment (residues 88-129) of domain I and the main loop (residues 65-73) in domain II exhibit large deviations in atomic positions when the solvent content is reduced, although the three-dimensional structure is essentially preserved. Many crucial water bridges between different regions of the molecule are conserved in spite of differences in detail, even when the level of hydration is reduced well below that required for activity. The loss of activity that accompany dehydration appears to be caused by the removal of functionally important water molecules from the active-site region and the reduction in the size of the substrate binding cleft.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9714162}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9714162 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9714162}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: O-glycosyl]]
[[Category: O-glycosyl]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:55:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:34:06 2008''

Revision as of 04:34, 29 July 2008

Image:1xei.png

Template:STRUCTURE 1xei

THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION

Template:ABSTRACT PUBMED 9714162

About this Structure

1XEI is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Role of water in plasticity, stability, and action of proteins: the crystal structures of lysozyme at very low levels of hydration., Nagendra HG, Sukumar N, Vijayan M, Proteins. 1998 Aug 1;32(2):229-40. PMID:9714162

Page seeded by OCA on Tue Jul 29 07:34:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xei"
Personal tools